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Predicate | Object |
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rdf:type | |
lifeskim:mentions | |
pubmed:issue |
4
|
pubmed:dateCreated |
1993-1-4
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pubmed:abstractText |
The cdc2 protein kinase, first identified as a cell cycle gene required for transition into the S- and M-phases of budding and fission yeast, has been shown to act as a key component in the regulation of the eukaryotic cell cycle. The periodic activation of cdc2 kinase, which is required for entry into M-phase, is regulated by subunit association with cyclin B, the cdc25, wee1, mik1 gene products and differential phosphorylation of the cdc2 protein. Phosphorylation at Tyr 15 inhibits activation of the cdc2/cdc13 complex whereas phosphorylation of Thr 167 is required for kinase activity.
|
pubmed:language |
eng
|
pubmed:journal | |
pubmed:citationSubset |
IM
|
pubmed:chemical | |
pubmed:status |
MEDLINE
|
pubmed:month |
Aug
|
pubmed:issn |
1043-4682
|
pubmed:author | |
pubmed:issnType |
Print
|
pubmed:volume |
2
|
pubmed:geneSymbol |
cdc2
|
pubmed:owner |
NLM
|
pubmed:authorsComplete |
Y
|
pubmed:pagination |
195-204
|
pubmed:dateRevised |
2009-11-19
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pubmed:meshHeading | |
pubmed:year |
1991
|
pubmed:articleTitle |
Regulation of cdc2 activity in Schizosaccharomyces pombe: the role of phosphorylation.
|
pubmed:affiliation |
Department of Cell Biology, School of Medicine, Vanderbilt University, Nashville, TN 37232.
|
pubmed:publicationType |
Journal Article,
Review
|