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http://purl.uniprot.org/citations/7607214http://www.w3.org/1999/02/22-rdf-syntax-ns#typehttp://purl.uniprot.org/core/Journal_Citation
http://purl.uniprot.org/citations/7607214http://www.w3.org/1999/02/22-rdf-syntax-ns#typehttp://purl.uniprot.org/core/Journal_Citation
http://purl.uniprot.org/citations/7607214http://www.w3.org/2000/01/rdf-schema#comment"We have revealed and characterised two nucleic-acid-binding proteins, termed PCBP-1 (M(r) 37,525, pI 7.07) and PCBP-2 (M(r) 38,579, pI 6.76), that together with heterogeneous ribonucleoparticle (hnRNP)-K correspond to the major cellular poly(rC)-binding proteins. mRNA for both PCBPs were detected in all the human tissues analysed. Both proteins contain three K-homologous (KH) domains which share similarity with other KH domain proteins, including the fragile-X protein FMR1, and which are positioned as in hnRNP-K and nova, i.e. with two closely spaced domains at the N-terminus and one at the C-terminus. PCBPs do not contain RGG boxes or any other known nucleic-acid-binding motifs. Expression in the vaccinia virus system showed that both proteins are post-translationally modified in vivo, a fact that was confirmed by [32P]orthophosphate labelling. Northwestern-blot analysis showed that the non-phosphorylated forms bind tenaciously to poly(rC) in vitro, while significantly less binding was observed for the phosphorylated variants. Escherichia coli expressed proteins also bound poly(rG), albeit at a lower level. In addition, PCBP-2 bound poly(rU), whereas very little binding to poly(rA) was observed for both proteins."xsd:string
http://purl.uniprot.org/citations/7607214http://purl.org/dc/terms/identifier"doi:10.1111/j.1432-1033.1995.tb20581.x"xsd:string
http://purl.uniprot.org/citations/7607214http://purl.org/dc/terms/identifier"doi:10.1111/j.1432-1033.1995.tb20581.x"xsd:string
http://purl.uniprot.org/citations/7607214http://purl.uniprot.org/core/author"Celis J.E."xsd:string
http://purl.uniprot.org/citations/7607214http://purl.uniprot.org/core/author"Celis J.E."xsd:string
http://purl.uniprot.org/citations/7607214http://purl.uniprot.org/core/author"Leffers H."xsd:string
http://purl.uniprot.org/citations/7607214http://purl.uniprot.org/core/author"Leffers H."xsd:string
http://purl.uniprot.org/citations/7607214http://purl.uniprot.org/core/author"Dejgaard K."xsd:string
http://purl.uniprot.org/citations/7607214http://purl.uniprot.org/core/author"Dejgaard K."xsd:string
http://purl.uniprot.org/citations/7607214http://purl.uniprot.org/core/date"1995"xsd:gYear
http://purl.uniprot.org/citations/7607214http://purl.uniprot.org/core/date"1995"xsd:gYear
http://purl.uniprot.org/citations/7607214http://purl.uniprot.org/core/name"Eur. J. Biochem."xsd:string
http://purl.uniprot.org/citations/7607214http://purl.uniprot.org/core/name"Eur. J. Biochem."xsd:string
http://purl.uniprot.org/citations/7607214http://purl.uniprot.org/core/pages"447-453"xsd:string
http://purl.uniprot.org/citations/7607214http://purl.uniprot.org/core/pages"447-453"xsd:string
http://purl.uniprot.org/citations/7607214http://purl.uniprot.org/core/title"Characterisation of two major cellular poly(rC)-binding human proteins, each containing three K-homologous (KH) domains."xsd:string
http://purl.uniprot.org/citations/7607214http://purl.uniprot.org/core/title"Characterisation of two major cellular poly(rC)-binding human proteins, each containing three K-homologous (KH) domains."xsd:string
http://purl.uniprot.org/citations/7607214http://purl.uniprot.org/core/volume"230"xsd:string
http://purl.uniprot.org/citations/7607214http://purl.uniprot.org/core/volume"230"xsd:string
http://purl.uniprot.org/citations/7607214http://www.w3.org/2004/02/skos/core#exactMatchhttp://purl.uniprot.org/pubmed/7607214
http://purl.uniprot.org/citations/7607214http://www.w3.org/2004/02/skos/core#exactMatchhttp://purl.uniprot.org/pubmed/7607214
http://purl.uniprot.org/citations/7607214http://xmlns.com/foaf/0.1/primaryTopicOfhttps://pubmed.ncbi.nlm.nih.gov/7607214
http://purl.uniprot.org/citations/7607214http://xmlns.com/foaf/0.1/primaryTopicOfhttps://pubmed.ncbi.nlm.nih.gov/7607214