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An additional, rarer mutation is a G→C transversion in exon 19 that results in an arginine to proline substitution and consequently, to disruption of a consensus serine/threonine kinase phosphorylation site (RIVT→PIVT) [4], suggesting that IKAP must be phosphorylated at certain domains to be fully active.
For example, a PPI could be achieved only if one of these proteins appears to be phosphorylated at certain residues.
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It is possible that the purified hMyo3A-KD is phosphorylated at certain sites prior to the autophosphorylation reaction.
KaiC is an autokinase and autophosphatase that can be phosphorylated at two adjacent residues: S431 and T432.
Paxillin, in contrast, was found to be phosphorylated at Tyr118 when membrane associated (Fig. 4b) and localized near ITGαVβ3 exclusively in AT-cells (Fig. 4c, arrowhead).
Yeast 26S proteasome has been shown to be phosphorylated at low stoichiometry (Wu et al., 2011).
Western analysis and chemical stability studies showed the AGT protein to be phosphorylated at tyrosine, threonine, and serine residues.
STX1 can be phosphorylated at residues other than Ser14.
P01233 can theoretically be phosphorylated at three sites.
In response to certain cytokines, NF-κB2 is phosphorylated at specific serine residues in its carboxyl-terminal region, leading to partial proteasomal degradation of the carboxyl terminus for the production of p52.
While Hsp90beta was phosphorylated at Ser 226/Ser 255 in untransformed cells, phosphorylation was absent in leukemic cells.
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