http://purl.uniprot.org/citations/14583602 | http://www.w3.org/1999/02/22-rdf-syntax-ns#type | http://purl.uniprot.org/core/Journal_Citation |
http://purl.uniprot.org/citations/14583602 | http://www.w3.org/1999/02/22-rdf-syntax-ns#type | http://purl.uniprot.org/core/Journal_Citation |
http://purl.uniprot.org/citations/14583602 | http://www.w3.org/2000/01/rdf-schema#comment | "The poly(A) tail shortening in mRNA, called deadenylation, is the first rate-limiting step in eukaryotic mRNA turnover, and the polyadenylate-binding protein (PABP) appears to be involved in the regulation of this step. However, the precise role of PABP remains largely unknown in higher eukaryotes. Here we identified and characterized a human PABP-dependent poly(A) nuclease (hPAN) complex consisting of catalytic hPan2 and regulatory hPan3 subunits. hPan2 has intrinsically a 3' to 5' exoribonuclease activity and requires Mg2+ for the enzyme activity. On the other hand, hPan3 interacts with PABP to simulate hPan2 nuclease activity. Interestingly, the hPAN nuclease complex has a higher substrate specificity to poly(A) RNA upon its association with PABP. Consistent with the roles of hPan2 and hPan3 in mRNA decay, the two subunits exhibit cytoplasmic co-localization. Thus, the human PAN complex is a poly(A)-specific exoribonuclease that is stimulated by PABP in the cytoplasm."xsd:string |
http://purl.uniprot.org/citations/14583602 | http://purl.org/dc/terms/identifier | "doi:10.1074/jbc.m309125200"xsd:string |
http://purl.uniprot.org/citations/14583602 | http://purl.org/dc/terms/identifier | "doi:10.1074/jbc.m309125200"xsd:string |
http://purl.uniprot.org/citations/14583602 | http://purl.uniprot.org/core/author | "Uchida N."xsd:string |
http://purl.uniprot.org/citations/14583602 | http://purl.uniprot.org/core/author | "Uchida N."xsd:string |
http://purl.uniprot.org/citations/14583602 | http://purl.uniprot.org/core/author | "Hoshino S."xsd:string |
http://purl.uniprot.org/citations/14583602 | http://purl.uniprot.org/core/author | "Hoshino S."xsd:string |
http://purl.uniprot.org/citations/14583602 | http://purl.uniprot.org/core/author | "Katada T."xsd:string |
http://purl.uniprot.org/citations/14583602 | http://purl.uniprot.org/core/author | "Katada T."xsd:string |
http://purl.uniprot.org/citations/14583602 | http://purl.uniprot.org/core/date | "2004"xsd:gYear |
http://purl.uniprot.org/citations/14583602 | http://purl.uniprot.org/core/date | "2004"xsd:gYear |
http://purl.uniprot.org/citations/14583602 | http://purl.uniprot.org/core/name | "J. Biol. Chem."xsd:string |
http://purl.uniprot.org/citations/14583602 | http://purl.uniprot.org/core/name | "J. Biol. Chem."xsd:string |
http://purl.uniprot.org/citations/14583602 | http://purl.uniprot.org/core/pages | "1383-1391"xsd:string |
http://purl.uniprot.org/citations/14583602 | http://purl.uniprot.org/core/pages | "1383-1391"xsd:string |
http://purl.uniprot.org/citations/14583602 | http://purl.uniprot.org/core/title | "Identification of a human cytoplasmic poly(A) nuclease complex stimulated by poly(A)-binding protein."xsd:string |
http://purl.uniprot.org/citations/14583602 | http://purl.uniprot.org/core/title | "Identification of a human cytoplasmic poly(A) nuclease complex stimulated by poly(A)-binding protein."xsd:string |
http://purl.uniprot.org/citations/14583602 | http://purl.uniprot.org/core/volume | "279"xsd:string |
http://purl.uniprot.org/citations/14583602 | http://purl.uniprot.org/core/volume | "279"xsd:string |
http://purl.uniprot.org/citations/14583602 | http://www.w3.org/2004/02/skos/core#exactMatch | http://purl.uniprot.org/pubmed/14583602 |
http://purl.uniprot.org/citations/14583602 | http://www.w3.org/2004/02/skos/core#exactMatch | http://purl.uniprot.org/pubmed/14583602 |
http://purl.uniprot.org/citations/14583602 | http://xmlns.com/foaf/0.1/primaryTopicOf | https://pubmed.ncbi.nlm.nih.gov/14583602 |
http://purl.uniprot.org/citations/14583602 | http://xmlns.com/foaf/0.1/primaryTopicOf | https://pubmed.ncbi.nlm.nih.gov/14583602 |