| pubmed-article:8332490 | rdf:type | pubmed:Citation | lld:pubmed |
| pubmed-article:8332490 | lifeskim:mentions | umls-concept:C0020792 | lld:lifeskim |
| pubmed-article:8332490 | lifeskim:mentions | umls-concept:C0035687 | lld:lifeskim |
| pubmed-article:8332490 | lifeskim:mentions | umls-concept:C0003765 | lld:lifeskim |
| pubmed-article:8332490 | lifeskim:mentions | umls-concept:C0036720 | lld:lifeskim |
| pubmed-article:8332490 | lifeskim:mentions | umls-concept:C1150423 | lld:lifeskim |
| pubmed-article:8332490 | lifeskim:mentions | umls-concept:C1514562 | lld:lifeskim |
| pubmed-article:8332490 | lifeskim:mentions | umls-concept:C1883221 | lld:lifeskim |
| pubmed-article:8332490 | lifeskim:mentions | umls-concept:C1521761 | lld:lifeskim |
| pubmed-article:8332490 | lifeskim:mentions | umls-concept:C0699759 | lld:lifeskim |
| pubmed-article:8332490 | lifeskim:mentions | umls-concept:C1883204 | lld:lifeskim |
| pubmed-article:8332490 | lifeskim:mentions | umls-concept:C1880389 | lld:lifeskim |
| pubmed-article:8332490 | pubmed:issue | 12 | lld:pubmed |
| pubmed-article:8332490 | pubmed:dateCreated | 1993-8-17 | lld:pubmed |
| pubmed-article:8332490 | pubmed:abstractText | The U1 snRNP-specific 70K protein is one of the few snRNP proteins from higher eukaryotic cells that is phosphorylated in vivo (1,2). Immunoaffinity purified spliceosomal snRNPs (U1, U2, U5, and U4/U6) were tested for their ability to phosphorylate in vitro the U1-specific 70K protein. An snRNP-associated kinase activity which phosphorylates all U1-70K isoelectric variants was identified. Like its in vivo counterpart, this snRNP-associated enzyme phosphorylates solely serine residues of the 70K protein, preferentially utilizing ATP as a phosphodonor. Tryptic phosphopeptide analysis revealed an overlapping set of at least four radiolabeled peptides in the in vivo and in vitro phosphorylated protein, suggesting that the snRNP-associated serine kinase is responsible, at least in part, for the 70K protein phosphorylation observed in vivo. Chymotryptic digestion of in vitro, 32P-labeled 70K protein and in vitro phosphorylation studies with a synthetic peptide, indicated that the multiple 70K phosphorylation sites are limited to a highly charged, C-terminal domain of the protein. In vitro phosphorylation studies with the splicing factor ASF/SF2 and several deletion mutants demonstrated that, similar to the U1-70K protein, the snRNP-associated serine kinase phosphorylates the carboxy terminal RS-rich domain of ASF/SF2. A potential general role for this enzyme in the phosphorylation of splicing factors and its consequences for pre-mRNA splicing regulation are discussed. | lld:pubmed |
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| pubmed-article:8332490 | pubmed:language | eng | lld:pubmed |
| pubmed-article:8332490 | pubmed:journal | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:8332490 | pubmed:citationSubset | IM | lld:pubmed |
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| pubmed-article:8332490 | pubmed:status | MEDLINE | lld:pubmed |
| pubmed-article:8332490 | pubmed:month | Jun | lld:pubmed |
| pubmed-article:8332490 | pubmed:issn | 0305-1048 | lld:pubmed |
| pubmed-article:8332490 | pubmed:author | pubmed-author:ManleyJ LJL | lld:pubmed |
| pubmed-article:8332490 | pubmed:author | pubmed-author:LührmannRR | lld:pubmed |
| pubmed-article:8332490 | pubmed:author | pubmed-author:ZukTT | lld:pubmed |
| pubmed-article:8332490 | pubmed:author | pubmed-author:KornstädtUU | lld:pubmed |
| pubmed-article:8332490 | pubmed:author | pubmed-author:WillC LCL | lld:pubmed |
| pubmed-article:8332490 | pubmed:author | pubmed-author:WoppmannAA | lld:pubmed |
| pubmed-article:8332490 | pubmed:issnType | Print | lld:pubmed |
| pubmed-article:8332490 | pubmed:day | 25 | lld:pubmed |
| pubmed-article:8332490 | pubmed:volume | 21 | lld:pubmed |
| pubmed-article:8332490 | pubmed:owner | NLM | lld:pubmed |
| pubmed-article:8332490 | pubmed:authorsComplete | Y | lld:pubmed |
| pubmed-article:8332490 | pubmed:pagination | 2815-22 | lld:pubmed |
| pubmed-article:8332490 | pubmed:dateRevised | 2009-11-19 | lld:pubmed |
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| pubmed-article:8332490 | pubmed:meshHeading | pubmed-meshheading:8332490-... | lld:pubmed |
| pubmed-article:8332490 | pubmed:year | 1993 | lld:pubmed |
| pubmed-article:8332490 | pubmed:articleTitle | Identification of an snRNP-associated kinase activity that phosphorylates arginine/serine rich domains typical of splicing factors. | lld:pubmed |
| pubmed-article:8332490 | pubmed:affiliation | Institut für Molekularbiologie und Tumorforschung, Marburg, Germany. | lld:pubmed |
| pubmed-article:8332490 | pubmed:publicationType | Journal Article | lld:pubmed |
| pubmed-article:8332490 | pubmed:publicationType | Research Support, Non-U.S. Gov't | lld:pubmed |
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