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Publication : Mouse p87wee1 kinase is regulated by M-phase specific phosphorylation.

First Author  Honda R Year  1995
Journal  Chromosome Res Volume  3
Issue  5 Pages  300-8
PubMed ID  7551544 Mgi Jnum  J:26519
Mgi Id  MGI:73964 Doi  10.1007/BF00713068
Citation  Honda R, et al. (1995) Mouse p87wee1 kinase is regulated by M-phase specific phosphorylation. Chromosome Res 3(5):300-8
abstractText  We have cloned a mouse wee1 kinase cDNA (mwee1). The clone is 2258 bp in length and its open reading frame corresponds to 646 amino acid residues. The molecular weight of this kinase is 87 kDa in SDS-PAGE, which is about 1.7-fold larger than the human p50wee1 kinase reported previously. In a cell cycle, the mouse wee1 kinase is phosphorylated at M-phase, and an in vitro study using a mitotic extract revealed that phosphorylation occurs in the N-terminal domain, which is absent from the human wee1 kinase, resulting in inactivation of the kinase activity. The N-terminal domain or entire molecule is extensively phosphorylated by cdc2-cyclin B kinase. Furthermore, the activity of the wee1 kinase was reduced by phosphorylation with the mitotic extract which contained cdc2-cyclin B kinase.
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