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Results 1 - 10 of 10
EC Number Posttranslational Modification Commentary Reference
Display the word mapDisplay the reaction diagram Show all sequences 3.4.24.87glycoprotein - 719163, 719761
Display the word mapDisplay the reaction diagram Show all sequences 3.4.24.87glycoprotein ADAMTS13 is a multidomain glycoprotein 711563
Display the word mapDisplay the reaction diagram Show all sequences 3.4.24.87glycoprotein binding site for alpha-mannosyl residue, 10 potential N-glycosylation sites, Asn-Xaa-Thr/Ser 652191
Display the word mapDisplay the reaction diagram Show all sequences 3.4.24.87glycoprotein enzym contains 10 potential N-glycosylation sites 652481
Display the word mapDisplay the reaction diagram Show all sequences 3.4.24.87glycoprotein N-glycosylation 653678
Display the word mapDisplay the reaction diagram Show all sequences 3.4.24.87glycoprotein N-glycosylation is necessary for efficient secretion of ADAMTS13, while conversion of the N-glycans from oligomannose to complex type in the Golgi complex enhances the proteolytic activity of the protease toward von Willebrand factor multimers. After its secretion, ADAMTS13 does not require N-glycans for its von Willebrand factor cleaving activity 691464
Display the word mapDisplay the reaction diagram Show all sequences 3.4.24.87glycoprotein the ADAMTS13 ancillary domains, ADAMTS13-DTCS, contain four potential N-glycosylation sites 710732
Display the word mapDisplay the reaction diagram Show all sequences 3.4.24.87proteolytic modification made as a zymogen, requires proteolytic activation, possibly intracellularly by furin, cleavage of residues 1-74 652191
Display the word mapDisplay the reaction diagram Show all sequences 3.4.24.87proteolytic modification propeptide is very short and poorly conserved, dispensable for protein folding, is cleaved off by furin after export from the endoplasmic reticulum, the pro-enzyme form is fully active 652481
Display the word mapDisplay the reaction diagram Show all sequences 3.4.24.87proteolytic modification the pro-peptide is removed during self-activation, which is not required for full enzyme activity 711809
Results 1 - 10 of 10