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EC Number Posttranslational Modification Commentary Reference
Display the word mapDisplay the reaction diagram Show all sequences 3.4.21.120glycoprotein - 668415, 669696, 670339, 670340
Display the word mapDisplay the reaction diagram Show all sequences 3.4.21.120glycoprotein contains terminal alpha-D-GalNAc and either terminal alpha-D-NeuAc or non-terminal beta-D-(GlcNAc)2 residues. Both the alpha- and beta-forms are sulphated on O-linked oligosaccharide side chains but are not phosphorylated. The hamster oviductin polymorphism is a consequence of different glycosylation patterns and not the polypeptide chain itself. Hamster oviductin is mostly O-glycosylated and contains a few N-linked oligosaccharide side chains (approx. 10 kDa). It is proposed that hamster oviductin is a mucin-type glycoprotein which might act as a protective secretion influencing the first steps of the reproductive process necessary for the normal triggering of fertilization and early embryonic development 667456
Display the word mapDisplay the reaction diagram Show all sequences 3.4.21.120glycoprotein glycosylation of hamster oviductin appears to be differentially regulated during the estrous cycle 667901
Display the word mapDisplay the reaction diagram Show all sequences 3.4.21.120glycoprotein mucin-type motifs 670339
Display the word mapDisplay the reaction diagram Show all sequences 3.4.21.120glycoprotein polymorphism in the heavily O-glycosylated region of hamster oviductin 667896
Display the word mapDisplay the reaction diagram Show all sequences 3.4.21.120glycoprotein the mature MOGP contained three potential N-linked glycosylation sites and 24 possible O-linked glycosylation sites -, 667897
Display the word mapDisplay the reaction diagram Show all sequences 3.4.21.120proteolytic modification protease is translated as the N terminus of an unusual mosaic protein. It is proposed that during post-translational proteolytic processing of the mosaic oviductin glycoprotein, the processed N-terminal protease domain is released coupled to two C-terminal CUB domains and constitutes the enzymatically active protease molecule 667898
Display the word mapDisplay the reaction diagram Show all sequences 3.4.21.120proteolytic modification translational products stored in the pars recta granules need to be processed to become a proteolytically active 66000 Da form. Extensive posttranslational processing for activation of proteolytic activity. Oviductin translated as 107.6-kDa precursors are processed both N- and C-terminally to give rise to a 66-kDa active form comprising a serine protease and two CUB domains 668362
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