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MGP003312

UniProt Annotations

Entry Information
Gene NameWEE1 G2 checkpoint kinase
Protein EntryWEE1_HUMAN
UniProt IDP30291
SpeciesHuman
Comments
Comment typeDescription
Alternative ProductsEvent=Alternative splicing; Named isoforms=2; Name=1; IsoId=P30291-1; Sequence=Displayed; Name=2; IsoId=P30291-2; Sequence=VSP_044959; Note=No experimental confirmation available.;
Catalytic ActivityATP + a [protein]-L-tyrosine = ADP + a [protein]-L-tyrosine phosphate. {ECO:0000255|PROSITE- ProRule:PRU10027}.
CofactorName=Mg(2+); Xref=ChEBI:CHEBI:18420; Note=Binds 2 magnesium ions per subunit.;
Enzyme RegulationSynthesis is increased during S and G2 phases, presumably by an increase in transcription; activity is decreased by phosphorylation during m phase. Protein levels fall in M phase as a result of decreased synthesis combined with degradation. Activity seems to be negatively regulated by phosphorylation upon entry into mitosis, although N-terminal phosphorylation might also regulate the protein stability via protection from proteolysis or might regulate the subcellular location.
FunctionActs as a negative regulator of entry into mitosis (G2 to M transition) by protecting the nucleus from cytoplasmically activated cyclin B1-complexed CDK1 before the onset of mitosis by mediating phosphorylation of CDK1 on 'Tyr-15'. Specifically phosphorylates and inactivates cyclin B1-complexed CDK1 reaching a maximum during G2 phase and a minimum as cells enter M phase. Phosphorylation of cyclin B1-CDK1 occurs exclusively on 'Tyr-15' and phosphorylation of monomeric CDK1 does not occur. Its activity increases during S and G2 phases and decreases at M phase when it is hyperphosphorylated. A correlated decrease in protein level occurs at M/G1 phase, probably due to its degradation.
InteractionQ9Y297:BTRC; NbExp=2; IntAct=EBI-914695, EBI-307461; Q9UKB1:FBXW11; NbExp=3; IntAct=EBI-914695, EBI-355189; P63104:YWHAZ; NbExp=3; IntAct=EBI-914695, EBI-347088;
PtmDephosphorylated at Thr-239 by CTDP1.
PtmPhosphorylated during M and G1 phases. Also autophosphorylated. Phosphorylation at Ser-642 by BRSK1 and BRSK2 in post-mitotic neurons, leads to down-regulate WEE1 activity in polarized neurons. Phosphorylated at Ser-53 and Ser-123 by PLK1 and CDK1, respectively, generating an signal for degradation that can be recognized by the SCF(BTRC) complex, leading to its ubiquitination and degradation at the onset of G2/M phase. {ECO:0000269|PubMed:15070733, ECO:0000269|PubMed:15150265, ECO:0000269|PubMed:18691976, ECO:0000269|PubMed:19690332, ECO:0000269|PubMed:20026642, ECO:0000269|PubMed:20068231, ECO:0000269|PubMed:22692537}.
PtmUbiquitinated and degraded at the onset of G2/M phase. {ECO:0000269|PubMed:15070733}.
SimilarityBelongs to the protein kinase superfamily. Ser/Thr protein kinase family. WEE1 subfamily. {ECO:0000255|PROSITE- ProRule:PRU00159}.
SimilarityContains 1 protein kinase domain. {ECO:0000255|PROSITE-ProRule:PRU00159}.
Subcellular LocationNucleus.
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