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Description

Wee1-like protein kinase (UniProt: P30291, also known as EC: 2.7.10.2, WEE1hu, Wee1A kinase) is encoded by the WEE1 gene (Gene ID: 7465) in human. Wee1 is a magnesium-dependent nuclear kinase that belongs to the Serine/Threonine family of protein kinases. It serves as a negative regulator of entry into mitosis (G2 to M transition) by protecting the nucleus from cytoplasmically activated cyclin B1-complexed Cdk1 prior to the onset of mitosis. Two isoforms of Wee1 have been described that are produced by alternative splicing. In isoform 1 the nucleotide binding site is localized to amino acids 305-313 and its protein kinase domain lies within amino acids 299-569. Wee1 specifically phosphorylates and inactivates cyclin B1-complexed Cdk1, reaching a maximum during G2 phase and a minimum as cells enter into M phase. Phosphorylation of cyclin B1-Cdk1 is shown to occur exclusively on Tyrosine 15. Wee1 levels are believed to increase during S and G2 phases due to increase in transcription and a decline in M phase has been attributed to reduced synthesis and higher degradation. Phosphorylation at serine 642 by BRSK1 and BRSK2 in post-mitotic neurons is reported to down-regulate Wee1 activity in polarized neurons. Also, phosphorylation at serine 53 by PLK1 and at serine 123 by Cdk1 generates a signal for its ubiquitination and proteasomal degradation at the onset of G2/M phase.