“…Since nonhistone acetylation was first identified, increasingly more functions for acetylation have been found to act on various life processes, including DNA damage response and autophagy (Botrugno et al ., ; Zhong et al ., ; Yasuda et al ., ), genomic stability (Billon et al ., ; Fournier and Tora, ), transcriptional activity (Seo et al ., ), protein degradation (Liu et al ., ; Wei et al ., ) and lysosomal function (Zhang et al ., ). Previous studies have shown that acetylation could compete with ubiquitination at the same lysine residue, thus blocking the ubiquitin‐mediated proteasomal degradation pathway to improve the protein stability, which is involved in cell cycle regulation (Lahusen et al ., ), tumour suppression and progression (Wan et al ., ; Choi et al ., ), bacterial virulence (Sang et al ., ) and signal transduction (Garcia‐Aguilar et al ., ; Beckwith et al ., ; Wei et al ., ). In our previous work, many acetylated sites were found on the nutrient storage proteins in the haemolymph of B. mori , including three storage proteins (SP1, SP2 and SP3), three apolipophorin proteins (BmApoLp‐I, BmApoLp‐II and BmApoLp‐III) and six 30 K proteins (Nie et al ., ).…”