Query author contributions in Reactome
Reactome depends on collaboration between our curation team and outside experts to assemble and peer-review its pathway modules. The integration of ORCID within Reactome enables us to meet a key challenge with authoring, curating and reviewing biological information by incentivizing and crediting the external experts that contribute their expertise and time to the Reactome curation process. More information is available at ORCID and Reactome.
If you have an ORCID ID that is not listed on this page, please forward this information to us and we will update your Reactome pathway records.
Details on Person After translation, many newly formed proteins undergo furthe...
| Class:Id | Summation:163842 |
|---|---|
| _displayName | After translation, many newly formed proteins undergo furthe... |
| _timestamp | 2017-08-22 22:09:07 |
| created | [InstanceEdit:163839] D'Eustachio, P, 2005-05-07 21:32:05 |
| modified | [InstanceEdit:164566] D'Eustachio, P, 2005-05-26 18:51:13 [InstanceEdit:9017591] D'Eustachio, Peter, 2017-08-22 [InstanceEdit:9017592] D'Eustachio, Peter, 2017-08-22 |
| text | After translation, many newly formed proteins undergo further covalent modifications that alter their functional properties. Modifications associated with protein localization include the attachment of oligosaccharide moieties to membrane-bound and secreted proteins (N-linked and O-linked glycosylation), the attachment of lipid (RAB geranylgeranylation) or glycolipid moieties (GPI-anchored proteins) that anchor proteins to cellular membranes, and the vitamin K-dependent attachment of carboxyl groups to glutamate residues. Modifications associated with functions of specific proteins include gamma carboxylation of clotting factors, hypusine formation on eukaryotic translation initiation factor 5A, conversion of a cysteine residue to formylglycine (arylsulfatase activation), methylation of lysine and arginine residues on non-histone proteins (protein methylation), protein phosphorylation by secretory pathway kinases, and carboxyterminal modifications of tubulin involving the addition of polyglutamate chains. Protein ubiquitination and deubiquitination play a major role in regulating protein stability and, together with SUMOylation and neddylation, can modulate protein function as well. |
| (summation) | [Pathway:597592] Post-translational protein modification [Homo sapiens] |
| [Change default viewing format] | |
