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Results 1 - 10 of 11 > >>
EC Number Posttranslational Modification Commentary Reference
Display the word mapDisplay the reaction diagram Show all sequences 3.6.5.3more differently from the wild-type enzyme the recombinant enzyme does not undergo post-translational modification of His603 into diphthamide, as indicated by its inability to be ADP-ribosylated 724476
Display the word mapDisplay the reaction diagram Show all sequences 3.6.5.3phosphoprotein heme-regulated inhibitor kinase-mediated phosphorylation of eukaryotic translation initiation factor 2 inhibits translation, induces stress granule formation, and mediates survival upon arsenite exposure 669326
Display the word mapDisplay the reaction diagram Show all sequences 3.6.5.3phosphoprotein IF2alpha is phosphorylated at Ser51 by four kinases in what is collectively known as the integrated stress response (ISR). Phosphorylation of Ser51 disrupts an intramolecular interaction between eIF2alpha-NTD and -CTD. This disruption exposes an eIF2B-binding surface on eIF2alpha-NTD that is otherwise obstructed by eIF2alpha-CTD. The intramolecular binding interface in eIF2alpha overlaps with the eIF2alpha binding surfaces for eIF2Bbeta, and possibly also eIF2Bdelta, in support of the hypothesis for an indirect effect of eIF2alpha phosphorylation on eIF2B-eIF2 binding. Phosphorylation destabilizes the eIF2alpha intramolecular interaction 757842
Display the word mapDisplay the reaction diagram Show all sequences 3.6.5.3phosphoprotein phosphorylation of the alpha-subunit of the eukaryotic initiation factor-2 (eIF2alpha) reduces protein synthesis and enhances apoptosis in response to proteasome inhibition 669316
Display the word mapDisplay the reaction diagram Show all sequences 3.6.5.3phosphoprotein recombinant subunits of eIF2alpha and beta-subunits are also phosphorylated in cultured insect cells. Phosphorylation of eIF2alpha in vitro is not significantly different in the presence and absence of the other subunits 670789
Display the word mapDisplay the reaction diagram Show all sequences 3.6.5.3proteolytic modification chymotrypsin degradation 644152
Display the word mapDisplay the reaction diagram Show all sequences 3.6.5.3proteolytic modification trypsin degradation 644162
Display the word mapDisplay the reaction diagram Show all sequences 3.6.5.3proteolytic modification trypsin degradation, four fragmentation products: 1 * 82000 + 1 * 48000 + 1 * 33000-34000 + 1 * 10000, SDS-PAGE 644151
Display the word mapDisplay the reaction diagram Show all sequences 3.6.5.3side-chain modification acetylation and methylation 644162
Display the word mapDisplay the reaction diagram Show all sequences 3.6.5.3side-chain modification methylation of lysine-56, enzyme with decreased rate of tRNA-dependent GTP hydrolysis 644149
Results 1 - 10 of 11 > >>