Sandbox GGC16
From Proteopedia
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A post-translational modification of PU.1 occurs at a serine residue (residue 41). This phosphorylation by protein kinase B (AKT) induces PU.1 activation.<ref>Rieske, P., & Pongubala, J. M. R. (2001). AKT Induces Transcriptional Activity of PU.1 through Phosphorylation-mediated Modifications within Its Transactivation Domain. Journal of Biological Chemistry, 276(11), 8460–8468. https://doi.org/10.1074/jbc.m007482200</ref> | A post-translational modification of PU.1 occurs at a serine residue (residue 41). This phosphorylation by protein kinase B (AKT) induces PU.1 activation.<ref>Rieske, P., & Pongubala, J. M. R. (2001). AKT Induces Transcriptional Activity of PU.1 through Phosphorylation-mediated Modifications within Its Transactivation Domain. Journal of Biological Chemistry, 276(11), 8460–8468. https://doi.org/10.1074/jbc.m007482200</ref> | ||
Revision as of 19:14, 24 April 2021
PU.1
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References
- ↑ UniProt ConsortiumEuropean Bioinformatics InstituteProtein Information ResourceSIB Swiss Institute of Bioinformatics. (2021, April 7). Transcription factor PU.1. UniProt ConsortiumEuropean Bioinformatics InstituteProtein Information ResourceSIB Swiss Institute of Bioinformatics. https://www.uniprot.org/uniprot/P17947.
- ↑ Rieske, P., & Pongubala, J. M. R. (2001). AKT Induces Transcriptional Activity of PU.1 through Phosphorylation-mediated Modifications within Its Transactivation Domain. Journal of Biological Chemistry, 276(11), 8460–8468. https://doi.org/10.1074/jbc.m007482200
- ↑ Kodandapani, R., Pio, F., Ni, CZ. et al. A new pattern for helix–turn–helix recognition revealed by the PU.l ETS–domain–DNA complex. Nature 380, 456–460 (1996). https://doi.org/10.1038/380456a0
- ↑ Mueller, B. U. Heterozygous PU.1 Mutations Are Associated with Acute Myeloid Leukemia. Blood. 2003, 101(5), 2074–2074.
