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| pubmed-article:1645449 | lifeskim:mentions | umls-concept:C0542341 | lld:lifeskim |
| pubmed-article:1645449 | lifeskim:mentions | umls-concept:C0079429 | lld:lifeskim |
| pubmed-article:1645449 | lifeskim:mentions | umls-concept:C1314939 | lld:lifeskim |
| pubmed-article:1645449 | lifeskim:mentions | umls-concept:C2003905 | lld:lifeskim |
| pubmed-article:1645449 | pubmed:issue | 6 | lld:pubmed |
| pubmed-article:1645449 | pubmed:dateCreated | 1991-7-3 | lld:pubmed |
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| pubmed-article:1645449 | pubmed:abstractText | The Saccharomyces cerevisiae SRK1 gene, when expressed on a low-copy shuttle vector, partially suppresses the phenotype associated with elevated levels of cyclic AMP-dependent protein kinase activity and suppresses the temperature-sensitive cell cycle arrest of the ins1 mutant. SRK1 is located on chromosome IV, 3 centimorgans from gcn2. A mutant carrying a deletion mutation in srk1 is viable. SRK1 encodes a 140-kDa protein with homology to the dis3+ protein from Schizosaccharomyces pombe. The ability of SRK1 to alleviate partially the defects caused by high levels of cyclic AMP-dependent protein kinase and the similarity of its encoded protein to dis3+ suggest that SRK1 may have a role in protein phosphatase function. | lld:pubmed |
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| pubmed-article:1645449 | pubmed:language | eng | lld:pubmed |
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| pubmed-article:1645449 | pubmed:citationSubset | IM | lld:pubmed |
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| pubmed-article:1645449 | pubmed:status | MEDLINE | lld:pubmed |
| pubmed-article:1645449 | pubmed:month | Jun | lld:pubmed |
| pubmed-article:1645449 | pubmed:issn | 0270-7306 | lld:pubmed |
| pubmed-article:1645449 | pubmed:author | pubmed-author:WilsonR BRB | lld:pubmed |
| pubmed-article:1645449 | pubmed:author | pubmed-author:EnglerM JMJ | lld:pubmed |
| pubmed-article:1645449 | pubmed:author | pubmed-author:TatchellKK | lld:pubmed |
| pubmed-article:1645449 | pubmed:author | pubmed-author:WhiteT BTB | lld:pubmed |
| pubmed-article:1645449 | pubmed:author | pubmed-author:BrennerA AAA | lld:pubmed |
| pubmed-article:1645449 | pubmed:author | pubmed-author:GaughranJ PJP | lld:pubmed |
| pubmed-article:1645449 | pubmed:issnType | Print | lld:pubmed |
| pubmed-article:1645449 | pubmed:volume | 11 | lld:pubmed |
| pubmed-article:1645449 | pubmed:geneSymbol | srk1 | lld:pubmed |
| pubmed-article:1645449 | pubmed:geneSymbol | ins1 | lld:pubmed |
| pubmed-article:1645449 | pubmed:geneSymbol | bcy1 | lld:pubmed |
| pubmed-article:1645449 | pubmed:geneSymbol | dis3+ | lld:pubmed |
| pubmed-article:1645449 | pubmed:owner | NLM | lld:pubmed |
| pubmed-article:1645449 | pubmed:authorsComplete | Y | lld:pubmed |
| pubmed-article:1645449 | pubmed:pagination | 3369-73 | lld:pubmed |
| pubmed-article:1645449 | pubmed:dateRevised | 2009-11-18 | lld:pubmed |
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| pubmed-article:1645449 | pubmed:year | 1991 | lld:pubmed |
| pubmed-article:1645449 | pubmed:articleTitle | The Saccharomyces cerevisiae SRK1 gene, a suppressor of bcy1 and ins1, may be involved in protein phosphatase function. | lld:pubmed |
| pubmed-article:1645449 | pubmed:affiliation | Department of Pathology and Laboratory Medicine, Hospital of the University of Pennsylvania, Philadelphia 19104-4283. | lld:pubmed |
| pubmed-article:1645449 | pubmed:publicationType | Journal Article | lld:pubmed |
| pubmed-article:1645449 | pubmed:publicationType | Comparative Study | lld:pubmed |
| pubmed-article:1645449 | pubmed:publicationType | Research Support, U.S. Gov't, P.H.S. | lld:pubmed |
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