| http://purl.uniprot.org/citations/12697755 | http://www.w3.org/1999/02/22-rdf-syntax-ns#type | http://purl.uniprot.org/core/Journal_Citation |
| http://purl.uniprot.org/citations/12697755 | http://www.w3.org/2000/01/rdf-schema#comment | "Inhibitor-2 (I-2) is a regulator of protein phosphatase type-1 (PP1), known to be phosphorylated in vitro by multiple kinases. In particular Thr72 is a Thr-Pro phosphorylation site conserved from yeast to human, but there is no evidence that this phosphorylation responds to any physiological signals. Here, we used electrophoretic mobility shift and immunoblotting with a site-specific phospho-Thr72 antibody to establish Thr72 phosphorylation in HeLa cells and show a 25-fold increase in phosphorylation during mitosis. Mass spectrometry demonstrated I-2 in actively growing HeLa cells was also phosphorylated at three other sites, Ser120, Ser121, and an additional Ser located between residues 70 and 90. In vitro kinase assays using recombinant I-2 as a substrate showed that the Thr72 kinase(s) was activated during mitosis, and sensitivity to kinase inhibitors indicated that the principal I-2 Thr72 kinase was not GSK3 but instead a member of the cyclin-dependent protein kinase family. Immunocytochemistry confirmed Thr72 phosphorylation of I-2 during mitosis, with peak intensity at prophase, and revealed subcellular concentration of the phospho-Thr72 I-2 at centrosomes. Together, the data show dynamic changes in I-2 phosphorylation during mitosis and localization of phosphorylated I-2 at centrosomes, suggesting involvement in mammalian cell division."xsd:string |
| http://purl.uniprot.org/citations/12697755 | http://purl.org/dc/terms/identifier | "doi:10.1074/jbc.m300782200"xsd:string |
| http://purl.uniprot.org/citations/12697755 | http://purl.uniprot.org/core/author | "Brautigan D.L."xsd:string |
| http://purl.uniprot.org/citations/12697755 | http://purl.uniprot.org/core/author | "Shenolikar S."xsd:string |
| http://purl.uniprot.org/citations/12697755 | http://purl.uniprot.org/core/author | "Leach C."xsd:string |
| http://purl.uniprot.org/citations/12697755 | http://purl.uniprot.org/core/date | "2003"xsd:gYear |
| http://purl.uniprot.org/citations/12697755 | http://purl.uniprot.org/core/name | "J Biol Chem"xsd:string |
| http://purl.uniprot.org/citations/12697755 | http://purl.uniprot.org/core/pages | "26015-26020"xsd:string |
| http://purl.uniprot.org/citations/12697755 | http://purl.uniprot.org/core/title | "Phosphorylation of phosphatase inhibitor-2 at centrosomes during mitosis."xsd:string |
| http://purl.uniprot.org/citations/12697755 | http://purl.uniprot.org/core/volume | "278"xsd:string |
| http://purl.uniprot.org/citations/12697755 | http://www.w3.org/2004/02/skos/core#exactMatch | http://purl.uniprot.org/pubmed/12697755 |
| http://purl.uniprot.org/citations/12697755 | http://xmlns.com/foaf/0.1/primaryTopicOf | https://pubmed.ncbi.nlm.nih.gov/12697755 |
| http://purl.uniprot.org/uniprot/#_P41236-mappedCitation-12697755 | http://www.w3.org/1999/02/22-rdf-syntax-ns#object | http://purl.uniprot.org/citations/12697755 |
| http://purl.uniprot.org/uniprot/P41236 | http://purl.uniprot.org/core/mappedCitation | http://purl.uniprot.org/citations/12697755 |