Proteolysis


Ontology type: npg:Subject  | skos:Concept     


Concept Info

NAME

Proteolysis

DESCRIPTION

Proteolysis is the enzymatic process by which proteins are degraded into their component polypeptide or amino acid parts. This generally occurs through protease-mediated hydrolysis of peptide bonds, but can also occur through non-enzymatic methods such as by action of mineral acids and heat.

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Download the RDF metadata as:  json-ld nt turtle xml License info

HOW TO GET THIS DATA PROGRAMMATICALLY:

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curl -H 'Accept: application/ld+json' 'https://scigraph.springernature.com/ontologies/subjects/proteolysis'

N-Triples is a line-based linked data format ideal for batch operations.

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

262 TRIPLES      9 PREDICATES      21 URIs      4 LITERALS

Subject Predicate Object
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4 skos:Concept
5 rdfs:label Proteolysis
6 skos:broader sg:ontologies/subjects/biochemistry
7 sg:ontologies/subjects/cell-biology
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9 skos:definition Proteolysis is the enzymatic process by which proteins are degraded into their component polypeptide or amino acid parts. This generally occurs through protease-mediated hydrolysis of peptide bonds, but can also occur through non-enzymatic methods such as by action of mineral acids and heat.
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15 sg:ontologies/subjects/proteasome
16 sg:ontologies/subjects/protein-quality-control
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18 sg:ontologies/subjects/ubiquitin-ligases
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20 skos:prefLabel Proteolysis
21 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.
22 dcterms:title Nature Subjects Taxonomy
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57 sg:ontologies/subjects/immunochemistry
58 sg:ontologies/subjects/ion-channels
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122 skos:broader sg:ontologies/subjects/proteolysis
123 skos:definition Deubiquitylating enzymes are proteases responsible for removing ubiquitin and ubiquitin chains from proteins. Deubiquitylating enzymes are either cysteine proteases or metalloproteases. As ubiquitylation of proteins can regulate their delivery to degradative proteasomes or to subcompartments of the cells, and regulate protein–protein interactions, deubiquitylating enzymes have consequences on substrate stability, localization and function.
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131 Endoplasmic reticulum associated degradation
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133 skos:broader sg:ontologies/subjects/proteolysis
134 skos:definition ER-associated degradation (ERAD) is the process by which the endoplasmic reticulum (ER) directs the degradation of misfolded or inappropriate proteins. The steps of ERAD include recognition of a misfolded protein – for instance for its inappropriate exposure of glycan residues – retro-translocation of the protein into the cytosol, and ubiquitin-dependent degradation by the proteasome.
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145 skos:definition Lysosomes are subcellular organelles that are mainly responsible for degradation of proteins internalized by cells by endocytosis and phagocytosis. Upon uptake, proteins and soluble components from the extracellular space pass through endosomes before fusing and/or maturing to form lysosomes. During the endosome–lysosome transition, the compartmental pH drops, which is conducive to the function of lysosomal acid hydrolases.
146 skos:inScheme sg:ontologies/subjects/
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155 Molecular Genetics
156 skos:broader sg:ontologies/subjects/biological-sciences
157 skos:definition Molecular Biology is the field of biology that studies the composition, structure and interactions of cellular molecules – such as nucleic acids and proteins – that carry out the biological processes essential for the cell’s functions and maintenance.
158 skos:inScheme sg:ontologies/subjects/
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162 sg:ontologies/subjects/crispr-cas-systems
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172 sg:ontologies/subjects/proteolysis
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184 sg:ontologies/subjects/neddylation sgo:sdDataset onto_subjects
185 rdf:type npg:Subject
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187 rdfs:label Neddylation
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189 sg:ontologies/subjects/proteolysis
190 skos:definition Neddylation is a post-translational modification process. It is analogous to ubiquitylation in terms of reaction scheme and enzyme classes used, but neddylated proteins are modified with the small ubiquitin-like protein NEDD8. The E1–E3 enzymes used are also distinct. Neddylation is known only for E3 ligases of the SCF class, so plays a role in ubiquitylation.
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198 26S Proteasome
199 Ingensin
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201 Macroxyproteinase
202 Multicatalytic Endopeptidase Complex
203 Multicatalytic Proteinase
204 Prosome
205 Proteasome Endopeptidase Complex
206 skos:broader sg:ontologies/subjects/proteolysis
207 skos:definition The proteasome is a large protein complex in the cytoplasm of eukaryotic and archaeal cells responsible for proteolysis of proteins that have one or more poly-ubiquitin post-translational modification. Structurally, proteasomes form a cylinder that consists of four stacked rings with a total molecular mass of ~2000 kDa.
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215 skos:definition Protein quality control is the mechanism by which a cell monitors proteins to ensure that they are appropriately folded. Protein quality control takes place predominantly in the endoplasmic reticulum, and can redeliver damaged proteins to the biosynthetic machinery or, failing correction, can deliver them to the ubiquitin–proteasome system for degradation.
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227 sg:ontologies/subjects/proteolysis
228 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.
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242 Ubiquitin-Protein Ligase E3
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245 skos:definition Ubiquitin ligases are enzymes involved in the ligation step of ubiquitylation. Ubiquitin ligases bind the substrate protein and catalyse the transfer of ubiquitin from the cysteine of ubiquitin-conjugating enzymes to a lysine residue on the substrate protein.
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255 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).
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