Sandbox GGC16: Difference between revisions
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=== Activation === | === Activation === | ||
<scene name='87/874948/Surfaceatmajorgroove/1'>Protein at Major Groove</scene> | |||
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> | ||
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Myeloid Leukemia. Blood. 2003, 101(5), 2074–2074.</ref> It is highly polar due to the abundance of proline, glutamate, serine, and threonine. Proteins with a PEST region typically have a short half-life of under 2 hours. It is hypothesized that the PEST region is a tag for fast degradation of the protein. | Myeloid Leukemia. Blood. 2003, 101(5), 2074–2074.</ref> It is highly polar due to the abundance of proline, glutamate, serine, and threonine. Proteins with a PEST region typically have a short half-life of under 2 hours. It is hypothesized that the PEST region is a tag for fast degradation of the protein. | ||
== References == | == References == | ||
<references/> | <references/> | ||
