Title : Akt regulates RSK2 to alter phosphorylation level of H2A.X in breast cancer.

Pub. Date : 2021 Mar

PMID : 33574926






2 Functional Relationships(s)
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1 The present study found that the activity of the serine/threonine kinase Akt was negatively associated with H2A.X phosphorylated at the Ser16 site (H2A.X S16ph), but the mechanism of the inverse relationship remains elusive. Serine AKT serine/threonine kinase 1 Homo sapiens
2 The current study indicated that the serine/threonine kinase ribosomal S6 kinase 2 (RSK2) as a kinase of H2A.X could be phosphorylated by Akt at Ser19 site. Serine AKT serine/threonine kinase 1 Homo sapiens