loading...| Preferred Name |
Post-translational protein modification |
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| Definitions |
Authored: D'Eustachio, P, 2005-04-18 15:58:56 Reviewed: Orlean, P, Stafford, DW, 0000-00-00 00:00:00 After translation, many newly formed proteins undergo further covalent modifications that alter their functional properties and that are essentially irreversible under physiological conditions in the body. These modifications include the internal peptide bond cleavages that activate proenzymes, the attachment of oligosaccharide moieties to membrane-bound and secreted proteins, the attachment of lipid or glycolipid moieties that serve to anchor proteins to cellular membranes, and the vitamin K-dependent attachment of carboxyl groups to glutamate residues. Edited: D'Eustachio, P, 0000-00-00 00:00:00 |
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| ID |
http://purl.obolibrary.org/obo/HINO_0016748 |
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| comment |
Authored: D'Eustachio, P, 2005-04-18 15:58:56 Reviewed: Orlean, P, Stafford, DW, 0000-00-00 00:00:00 After translation, many newly formed proteins undergo further covalent modifications that alter their functional properties and that are essentially irreversible under physiological conditions in the body. These modifications include the internal peptide bond cleavages that activate proenzymes, the attachment of oligosaccharide moieties to membrane-bound and secreted proteins, the attachment of lipid or glycolipid moieties that serve to anchor proteins to cellular membranes, and the vitamin K-dependent attachment of carboxyl groups to glutamate residues. Edited: D'Eustachio, P, 0000-00-00 00:00:00 |
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| definition source |
Reactome, http://www.reactome.org |
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| label |
Post-translational protein modification |
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| prefixIRI |
HINO:0016748 |
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| prefLabel |
Post-translational protein modification |
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| seeAlso |
GENE ONTOLOGYGO:0043687 Reactome Database ID Release 43597592 ReactomeREACT_22161 |
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| subClassOf | ||
| has_part |
http://purl.obolibrary.org/obo/HINO_0016736 http://purl.obolibrary.org/obo/HINO_0016810 |