loading...| Preferred Name |
PTM: gamma carboxylation, hypusine formation and arylsulfatase activation |
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| Definitions |
Authored: D'Eustachio, P, 2005-05-07 21:32:05 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 vitamin K-dependent attachment of carboxyl groups to glutamate residues and the conversion of lysine residues to hypusine. Edited: D'Eustachio, P, 0000-00-00 00:00:00 |
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http://purl.obolibrary.org/obo/HINO_0016725 |
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| comment |
Authored: D'Eustachio, P, 2005-05-07 21:32:05 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 vitamin K-dependent attachment of carboxyl groups to glutamate residues and the conversion of lysine residues to hypusine. 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 |
PTM: gamma carboxylation, hypusine formation and arylsulfatase activation |
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| prefixIRI |
HINO:0016725 |
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| prefLabel |
PTM: gamma carboxylation, hypusine formation and arylsulfatase activation |
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| seeAlso |
ReactomeREACT_1069 Reactome Database ID Release 43163841 GENE ONTOLOGYGO:0043687 |
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| has_part |
http://purl.obolibrary.org/obo/HINO_0016723 |