Post-translational modifications


Ontology type: npg:Subject  | skos:Concept     


Concept Info

NAME

Post-translational modifications

DESCRIPTION

Post-translational modifications are modifications that occur on a protein, catalysed by enzymes, after its translation by ribosomes is complete. Post-translational modification generally refers to the addition of a functional group covalently to a protein as in phosphorylation and neddylation, but also refers to proteolytic processing and folding processes necessary for a protein to mature functionally.

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This table displays all metadata directly associated to this object as RDF triples.

276 TRIPLES      10 PREDICATES      35 URIs      17 LITERALS

Subject Predicate Object
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2 sgo:sdDataset onto_subjects
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7 Post Translational Modifications
8 Post Translational Protein Modification
9 Post Translational Protein Processing
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11 Post-Translational Modification
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22 skos:definition Post-translational modifications are modifications that occur on a protein, catalysed by enzymes, after its translation by ribosomes is complete. Post-translational modification generally refers to the addition of a functional group covalently to a protein as in phosphorylation and neddylation, but also refers to proteolytic processing and folding processes necessary for a protein to mature functionally.
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35 sg:ontologies/subjects/ dcterms:description The Nature Subjects Taxonomy is a polyhierarchical categorization of scholarly subject areas which are used for the indexing of content by Springer Nature.
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54 skos:definition Acetylation is any chemical reaction that adds an acetyl chemical group (CH3C=O, sometimes abbreviated in chemical structures as Ac) and is a type of acylation reaction. Acetylation of proteins, generally on lysine residues, via an acetyl-coenzyme A donor, can have functional consequences, as in proteins contained within chromatin and metabolic enzymes.
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154 skos:definition Glycosylation is the reaction catalysed by glycosyltransferases, which adds carbohydrates site-specifically to another molecule, generally proteins and lipids. Glycosylation comes in five forms: N-linked, O-linked and phospho–serine glycosylation, as well as C-mannosylation and glypation (addition of glycophosphatidylinositol). Glycosylation can help a protein achieve folding and can facilitate signalling and cell–cell adhesion.
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163 skos:definition Methylation is any chemical reaction that adds a methyl chemical group (CH3, sometimes abbreviated in chemical structures as Me). In biology, it is a post-translational modification that occurs on proteins, such as histones, on the lysine and arginine residues. Methylation of DNA at target sequences plays an important role in gene regulation.
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226 skos:definition Phosphorylation is the enzymatic process through which a phosphate group is added via an ester bond, generally by a kinase, to either a small molecule or a protein. Protein phosphorylation is important in regulating signal transduction systems, as it affects the activity of its target, for instance in turning an enzyme ‘on’ or ‘off’.
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231 skos:Concept
232 rdfs:label PolyADP-ribosylation
233 skos:altLabel Parylation
234 skos:broader sg:ontologies/subjects/post-translational-modifications
235 skos:definition PolyADP-ribosylation, also known as parylation, is the post-translational modification process by which polymers of ADP-ribose (poly(adenosinediphosphate-ribose)) are covalently attached to proteins by PAR polymerase enzymes. The polymerase covalently attaches poly(ADP-ribose) polymer to itself and appropriate acceptors such as histones and other DNA-associated proteins. Parylation regulates chromatin organization, DNA repair, transcription and replication and other processes.
236 skos:inScheme sg:ontologies/subjects/
237 skos:prefLabel PolyADP-ribosylation
238 sg:ontologies/subjects/prenylation sgo:sdDataset onto_subjects
239 rdf:type npg:Subject
240 skos:Concept
241 rdfs:label Prenylation
242 skos:altLabel Farnesylation
243 Geranylgeranylation
244 Isoprenylation
245 skos:broader sg:ontologies/subjects/post-translational-modifications
246 skos:definition Prenylation is the post-translational modification process in which either a farnesyl group, as in farnesylation, or a geranyl-geranyl group, as in geranylgeranylation, is added to a C-terminal cysteine residue of the target protein. Prenylation can be catalysed by farnesyl transferase, Caax protease or geranylgeranyl transferases.
247 skos:inScheme sg:ontologies/subjects/
248 skos:prefLabel Prenylation
249 sg:ontologies/subjects/sumoylation sgo:sdDataset onto_subjects
250 rdf:type npg:Subject
251 skos:Concept
252 rdfs:label Sumoylation
253 skos:altLabel SUMO Conjugation
254 SUMO-Conjugation
255 SUMO-Conjugations
256 Sumoylations
257 skos:broader sg:ontologies/subjects/post-translational-modifications
258 sg:ontologies/subjects/proteolysis
259 skos:definition Sumoylation is a post-translational modification process. It is analogous to ubiquitylation in terms of the reaction scheme and enzyme classes used, but rather than conjugation by ubiquitin, sumoylation involves addition of SUMOs (small ubiquitin-like modifiers). Sumoylation can affect a protein’s structure and subcellular localization.
260 skos:inScheme sg:ontologies/subjects/
261 skos:prefLabel Sumoylation
262 sg:ontologies/subjects/ubiquitylation sgo:sdDataset onto_subjects
263 rdf:type npg:Subject
264 skos:Concept
265 rdfs:label Ubiquitylation
266 skos:altLabel Ubiquitination
267 skos:broader sg:ontologies/subjects/post-translational-modifications
268 sg:ontologies/subjects/proteolysis
269 skos:definition Ubiquitylation is the post-translational modification process by which ubiquitin is attached via an isopeptide bond to lysine residues on a protein. Ubiquitylation consists of three steps, activation by ubiquitin-activating enzymes (E1 enzymes), conjugation by ubiquitin-conjugating enzymes (E2s) and attachment to the substrate protein by ubiquitin ligases (E3s).
270 skos:inScheme sg:ontologies/subjects/
271 skos:prefLabel Ubiquitylation
272 skos:Concept sgo:sdDataset for_codes
273 rdf:type rdfs:Class
274 rdfs:Resource
275 rdfs:subClassOf rdfs:Resource
276 skos:Concept
 




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