CDK1 phosphorylates Mastl Authored: Orlic-Milacic, M, 2012-09-04 EC Number: 2.7.11.22 Edited: Gillespie, ME, 2012-09-14 Phosphorylation of MASTL (GWL) by CDK1 (Cdc2) was established using Mastl (Gwl) purified from Xenopus egg extracts and recombinant human CDK1. Phosphopeptide mapping identified several CDK1 phosphorylation sites in Mastl of which threonine residues T193 (Blake-Hodek et al. 2012), T206 (Blake-Hodek et al. 2012) and T748 (Yu et al. 2006) were found to be functionally important. These threonine residues are conserved and they correspond to T194, T207 and T741 of human MASTL. In addition, phosphorylation of Xenopus Mastl on serines S101 and S883 is important for the mitotic function of Mastl, but these sites, although conserved in Xenopus, human and mouse, do not conform to the CDK1 consensus, and the responsible kinase has not been identified. S883 may represent an autophosphorylation site (Blake-Hodek et al. 2012). Pubmed16600872 Pubmed22354989 Reactome Database ID Release 432434198 Reactome, http://www.reactome.org ReactomeREACT_150132 Reviewed: Burgess, A, 2012-09-28 Reviewed: Mochida, Satoru, 2012-09-26 has a Stoichiometric coefficient of 3