| http://purl.uniprot.org/citations/12504901 | http://www.w3.org/1999/02/22-rdf-syntax-ns#type | http://purl.uniprot.org/core/Journal_Citation |
| http://purl.uniprot.org/citations/12504901 | http://www.w3.org/1999/02/22-rdf-syntax-ns#type | http://purl.uniprot.org/core/Journal_Citation |
| http://purl.uniprot.org/citations/12504901 | http://www.w3.org/2000/01/rdf-schema#comment | "The yeast (Saccharomyces cerevisiae) contains three N-acetyltransferases, NatA, NatB, and NatC, each of which acetylates proteins with different N-terminal regions. The 19S regulatory particle of the yeast 26S proteasome consists of 17 subunits, 12 of which are N-terminally modified. By using nat1, nat3, and mak3 deletion mutants, we found that 8 subunits, Rpt4, Rpt5, Rpt6, Rpn2, Rpn3, Rpn5, Rpn6, and Rpn8, were NatA substrates, and that 2 subunits, Rpt3 and Rpn11, were NatB substrates. Mass spectrometric analysis revealed that the initiator Met of Rpt2 precursor polypeptide was processed and a part of the mature Rpt2 was N-myristoylated. The crude extracts from the normal strain and the nat1 deletion mutant were similar in chymotrypsin-like activity in the presence of ATP in vitro and in the accumulation level of the 26S proteasome. These characteristics were different from those of the 20S proteasome: the chymotrypsin-like activity and accumulation level of 20S proteasome were appreciably higher from the nat1 deletion mutant than from the normal strain."xsd:string |
| http://purl.uniprot.org/citations/12504901 | http://purl.org/dc/terms/identifier | "doi:10.1016/s0003-9861(02)00639-2"xsd:string |
| http://purl.uniprot.org/citations/12504901 | http://purl.org/dc/terms/identifier | "doi:10.1016/s0003-9861(02)00639-2"xsd:string |
| http://purl.uniprot.org/citations/12504901 | http://purl.uniprot.org/core/author | "Hirano H."xsd:string |
| http://purl.uniprot.org/citations/12504901 | http://purl.uniprot.org/core/author | "Hirano H."xsd:string |
| http://purl.uniprot.org/citations/12504901 | http://purl.uniprot.org/core/author | "Kimura Y."xsd:string |
| http://purl.uniprot.org/citations/12504901 | http://purl.uniprot.org/core/author | "Kimura Y."xsd:string |
| http://purl.uniprot.org/citations/12504901 | http://purl.uniprot.org/core/author | "Polevoda B."xsd:string |
| http://purl.uniprot.org/citations/12504901 | http://purl.uniprot.org/core/author | "Polevoda B."xsd:string |
| http://purl.uniprot.org/citations/12504901 | http://purl.uniprot.org/core/author | "Sherman F."xsd:string |
| http://purl.uniprot.org/citations/12504901 | http://purl.uniprot.org/core/author | "Sherman F."xsd:string |
| http://purl.uniprot.org/citations/12504901 | http://purl.uniprot.org/core/author | "Saeki Y."xsd:string |
| http://purl.uniprot.org/citations/12504901 | http://purl.uniprot.org/core/author | "Saeki Y."xsd:string |
| http://purl.uniprot.org/citations/12504901 | http://purl.uniprot.org/core/author | "Yokosawa H."xsd:string |
| http://purl.uniprot.org/citations/12504901 | http://purl.uniprot.org/core/author | "Yokosawa H."xsd:string |
| http://purl.uniprot.org/citations/12504901 | http://purl.uniprot.org/core/date | "2003"xsd:gYear |
| http://purl.uniprot.org/citations/12504901 | http://purl.uniprot.org/core/date | "2003"xsd:gYear |
| http://purl.uniprot.org/citations/12504901 | http://purl.uniprot.org/core/name | "Arch. Biochem. Biophys."xsd:string |
| http://purl.uniprot.org/citations/12504901 | http://purl.uniprot.org/core/name | "Arch. Biochem. Biophys."xsd:string |
| http://purl.uniprot.org/citations/12504901 | http://purl.uniprot.org/core/pages | "341-348"xsd:string |
| http://purl.uniprot.org/citations/12504901 | http://purl.uniprot.org/core/pages | "341-348"xsd:string |
| http://purl.uniprot.org/citations/12504901 | http://purl.uniprot.org/core/title | "N-terminal modifications of the 19S regulatory particle subunits of the yeast proteasome."xsd:string |
| http://purl.uniprot.org/citations/12504901 | http://purl.uniprot.org/core/title | "N-terminal modifications of the 19S regulatory particle subunits of the yeast proteasome."xsd:string |