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Publication : Novel homeodomain-interacting protein kinase family member, HIPK4, phosphorylates human p53 at serine 9.

First Author  Arai S Year  2007
Journal  FEBS Lett Volume  581
Issue  29 Pages  5649-57
PubMed ID  18022393 Mgi Jnum  J:127713
Mgi Id  MGI:3764736 Doi  10.1016/j.febslet.2007.11.022
Citation  Arai S, et al. (2007) Novel homeodomain-interacting protein kinase family member, HIPK4, phosphorylates human p53 at serine 9. FEBS Lett 581(29):5649-57
abstractText  We describe here the cloning and characterization of a novel mouse homeodomain-interacting protein kinase (HIPK)-like gene, Hipk4. Hipk4 is expressed in lung and in white adipose tissue and encodes a 616 amino acid protein that includes a serine/threonine kinase domain. We demonstrate that HIPK4 could phosphorylate human p53 protein at serine 9, both in vitro and in vivo. Among known p53-responsive promoters, activity of the human survivin promoter, which is repressed by p53, was decreased by HIPK4 in p53 functional A549 cells. Human BCL2-associated X protein-promoter activity was not affected. These findings suggest that phosphorylation of p53 at serine 9 is important for p53 mediated transcriptional repression.
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