Non-histone protein acetylation is involved in key cellular processes relevant to physiology and disease, such as gene transcription, DNA damage repair, cell division, signal transduction, protein folding, autophagy and metabolism.
One such example I may think of is the DNA Damage Response (DDR) process where non-histone acetylation has been found. When inducing DNA damage in human cells, the acetylation of lysine 382 and phosphorylation of serine 392 in p53, a key DDR factor, can significantly enhance the interaction between p53 and MDC1 and promote the recruitment of these two proteins to DNA damage sites.
Attached below are a few references which you may want to refer for more information.
Article Acetylation of Lysine 382 and Phosphorylation of Serine 392 ...
Article NAT10 regulates p53 activation through acetylating p53 at K1...
Article Sun, Y., Jiang, X., Chen, S., Fernandes, N. & Price, B. D. A...
Methylation of some non-histone proteins, such as NF-κB, p53, pCAF, ERα, and several transcription factors, has been known to affect protein stability, activity, and functions, which contribute to tumorigenesis, immunogenicity, and inflammation during tumorous and infectious diseases.
Attached below are a few references which may help.
Article Emerging roles of lysine methylation on non-histone proteins
Article Methylation, a new epigenetic mark for protein stability