Morphological changes in diabetic kidney are associated with increased O-GlcNAcylation of cytoskeletal proteins including α-actinin 4

Table 2 Comparison between phosphorylation sites and O-GlcNAcylation sites

Protein	Phosphorylation sites	O-GlcNAcylation sites
actin	S35, S201²⁷	S54, S157, S201, S234, S370²⁶
α-actinin 4	Y265, S423, S621, K625, T667^{27, 30}	S262, S269, T612, S613, S656*
α-tubulin	Y103, Y224, S232, Y272, T334^{35, 36}	S6, S158, S178, T271, S419**
myosin heavy chain	Y389, Y410, S949, S1038, Y1375 Y1415, Y1852, S1956, T1960^{39, 40}	S172, S179, S196, S392, S622, S626, S643, S644, S749, S880, S1038, S1102, S1148, S1159, S1189, S1200, S1299, S1308, S1336, S1470, S1471, S1596, S1597, S1600, S1606, S1710, S1711, S1777, S1916²⁶

Boldface type indicates the site at which O-GlcNAcylation and O-phosphorylation compete or their respective sites that are close to each other.
* Predicted by YinOYang1.2 prediction server http://www.cbs.dtu.dk/services/YinOYang/
* * Predicted by dbOGAP prediction server https://cbsb.lombardi.georgetown.edu/OGAP.html

ISSN: 1559-0275