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http://purl.uniprot.org/citations/17880284http://www.w3.org/1999/02/22-rdf-syntax-ns#typehttp://purl.uniprot.org/core/Journal_Citation
http://purl.uniprot.org/citations/17880284http://www.w3.org/1999/02/22-rdf-syntax-ns#typehttp://purl.uniprot.org/core/Journal_Citation
http://purl.uniprot.org/citations/17880284http://www.w3.org/2000/01/rdf-schema#comment"At least two of the genes predicted to encode type II PI4K (phosphoinositide 4-kinase) in Arabidopsis thaliana (thale cress), namely AtPI4Kgamma4 and AtPI4Kgamma7, encode enzymes with catalytic properties similar to those of members of the PIKK (phosphoinositide kinase-related kinase) family. AtPI4Kgamma4 and AtPI4Kgamma7 undergo autophosphorylation and phosphorylate serine/threonine residues of protein substrates, but have no detectable lipid kinase activity. AtPI4Kgamma4 and AtPI4Kgamma7 are members of a subset of five putative AtPI4Ks that contain N-terminal UBL (ubiquitin-like) domains. In vitro analysis of AtPI4Kgamma4 indicates that it interacts directly with, and phosphorylates, two proteins involved in the ubiquitin-proteasome system, namely UFD1 (ubiquitin fusion degradation 1) and RPN10 (regulatory particle non-ATPase 10). On the basis of the present results, we propose that AtPI4Kgamma4 and AtPI4Kgamma7 should be designated UbDKgamma4 and UbDKgamma7 (ubiquitin-like domain kinases gamma4 and gamma7). These UBL-domain-containing AtPI4Ks correspond to a new PIKK subfamily of protein kinases. Furthermore, UFD1 and RPN10 phosphorylation represents an additional mechanism by which their function can be regulated."xsd:string
http://purl.uniprot.org/citations/17880284http://purl.org/dc/terms/identifier"doi:10.1042/bj20070959"xsd:string
http://purl.uniprot.org/citations/17880284http://purl.org/dc/terms/identifier"doi:10.1042/bj20070959"xsd:string
http://purl.uniprot.org/citations/17880284http://purl.uniprot.org/core/author"Soderblom E.J."xsd:string
http://purl.uniprot.org/citations/17880284http://purl.uniprot.org/core/author"Soderblom E.J."xsd:string
http://purl.uniprot.org/citations/17880284http://purl.uniprot.org/core/author"Goshe M.B."xsd:string
http://purl.uniprot.org/citations/17880284http://purl.uniprot.org/core/author"Goshe M.B."xsd:string
http://purl.uniprot.org/citations/17880284http://purl.uniprot.org/core/author"Kota U."xsd:string
http://purl.uniprot.org/citations/17880284http://purl.uniprot.org/core/author"Kota U."xsd:string
http://purl.uniprot.org/citations/17880284http://purl.uniprot.org/core/author"Boss W.F."xsd:string
http://purl.uniprot.org/citations/17880284http://purl.uniprot.org/core/author"Boss W.F."xsd:string
http://purl.uniprot.org/citations/17880284http://purl.uniprot.org/core/author"Galvao R.M."xsd:string
http://purl.uniprot.org/citations/17880284http://purl.uniprot.org/core/author"Galvao R.M."xsd:string
http://purl.uniprot.org/citations/17880284http://purl.uniprot.org/core/date"2008"xsd:gYear
http://purl.uniprot.org/citations/17880284http://purl.uniprot.org/core/date"2008"xsd:gYear
http://purl.uniprot.org/citations/17880284http://purl.uniprot.org/core/name"Biochem. J."xsd:string
http://purl.uniprot.org/citations/17880284http://purl.uniprot.org/core/name"Biochem. J."xsd:string
http://purl.uniprot.org/citations/17880284http://purl.uniprot.org/core/pages"117-127"xsd:string
http://purl.uniprot.org/citations/17880284http://purl.uniprot.org/core/pages"117-127"xsd:string
http://purl.uniprot.org/citations/17880284http://purl.uniprot.org/core/title"Characterization of a new family of protein kinases from Arabidopsis containing phosphoinositide 3/4-kinase and ubiquitin-like domains."xsd:string
http://purl.uniprot.org/citations/17880284http://purl.uniprot.org/core/title"Characterization of a new family of protein kinases from Arabidopsis containing phosphoinositide 3/4-kinase and ubiquitin-like domains."xsd:string
http://purl.uniprot.org/citations/17880284http://purl.uniprot.org/core/volume"409"xsd:string
http://purl.uniprot.org/citations/17880284http://purl.uniprot.org/core/volume"409"xsd:string