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p(MESH:Proteins, pmod(Ub))

Equivalencies: 0 | Classes: 0 | Children: 0 | Explore

Entity

Name
Proteins
Namespace
MeSH
Namespace Version
20181007
Namespace URL
https://raw.githubusercontent.com/pharmacome/terminology/01c9daa61012b37dd0a1bc962521ba51a15b38f1/external/mesh-names.belns

Appears in Networks 4

The Ubiquitin Proteasome System in Neurodegenerative Diseases: Sometimes the Chicken, Sometimes the Egg v1.0.0

Perilous journey: a tour of the ubiquitin–proteasome system v1.0.0

The Ubiquitin–Proteasome System and the Autophagic–Lysosomal System in Alzheimer Disease v1.0.0

Autophagy and the ubiquitin-proteasome system: collaborators in neuroprotection v1.0.0

In-Edges 15

p(MESH:Proteins) hasVariant p(MESH:Proteins, pmod(Ub)) View Subject | View Object

Appears in Networks:

p(UNIPROT:P32628) increases tloc(p(MESH:Proteins, pmod(Ub)), fromLoc(GO:cytosol), toLoc(GO:"proteasome complex")) View Subject | View Object

Thus, Rad23 and Dsk2 in yeast are believed to bind polyubiquitinated substrates in the cytosol and target them to the proteasome PubMed:14556719

Appears in Networks:

p(UNIPROT:P48510) increases tloc(p(MESH:Proteins, pmod(Ub)), fromLoc(GO:cytosol), toLoc(GO:"proteasome complex")) View Subject | View Object

Thus, Rad23 and Dsk2 in yeast are believed to bind polyubiquitinated substrates in the cytosol and target them to the proteasome PubMed:14556719

Appears in Networks:

complex(a(GO:"proteasome complex"), p(MESH:Proteins, pmod(Ub))) hasComponent p(MESH:Proteins, pmod(Ub)) View Subject | View Object

Appears in Networks:

a(GO:lysosome) increases deg(p(MESH:Proteins, pmod(Ub))) View Subject | View Object

It has recently become appreciated that ubiquitination of proteins by covalent modification tags them for elimination not only through the proteasome (the ubiquitin–proteasome system or UPS) but also through the lysosomal system. PubMed:22908190

Appears in Networks:

bp(GO:"lysosomal protein catabolic process") decreases p(MESH:Proteins, pmod(Ub)) View Subject | View Object

In APP transgenic mouse models of AD, undigested autophagy substrates including LC3-II, p62, and ubiquitinated proteins accumulate in neuronal AVs, establishing that autophagic protein turnover in lysosomes is impeded (Yang et al. 2011). PubMed:22908190

Appears in Networks:
Annotations
MeSH
Alzheimer Disease

bp(GO:"proteasome-mediated ubiquitin-dependent protein catabolic process") increases deg(p(MESH:Proteins, pmod(Ub))) View Subject | View Object

It has recently become appreciated that ubiquitination of proteins by covalent modification tags them for elimination not only through the proteasome (the ubiquitin–proteasome system or UPS) but also through the lysosomal system. PubMed:22908190

Appears in Networks:

complex(GO:"proteasome complex") increases deg(p(MESH:Proteins, pmod(Ub))) View Subject | View Object

The proteasome selectively degrades normal proteins (mainly those with short half-lives) and abnormal proteins, which are earmarked for elimination by a process involving their conjugation to ubiquitin (Ub; Goldberg 2003). PubMed:22908190

Appears in Networks:

complex(a(GO:"proteasome regulatory particle"), p(MESH:Proteins, pmod(Ub))) hasComponent p(MESH:Proteins, pmod(Ub)) View Subject | View Object

Appears in Networks:

p(MESH:Proteins, pmod(Ub)) increases deg(p(MESH:Proteins, pmod(Ub))) View Subject | View Object

Third, there is ligation of Ub with an epsilon-amino group of lysine in the target protein by an E3 ligase. E3 ligase binds both the target protein and the E2–Ub complex; thousands of substrate- specific E3s ensure selective protein tagging and degradation. PubMed:22908190

Appears in Networks:

complex(a(MESH:Proteins), a(MESH:Ubiquitin), p(HGNC:UBA2), p(HGNC:UBA3)) increases p(MESH:Proteins, pmod(Ub)) View Subject | View Object

Third, there is ligation of Ub with an epsilon-amino group of lysine in the target protein by an E3 ligase. E3 ligase binds both the target protein and the E2–Ub complex; thousands of substrate- specific E3s ensure selective protein tagging and degradation. PubMed:22908190

Appears in Networks:

complex(p(HGNC:UBQLN1), p(MESH:Proteins, pmod(Ub))) hasComponent p(MESH:Proteins, pmod(Ub)) View Subject | View Object

Appears in Networks:

composite(a(CHEBI:lactacystin), a(CHEBI:sirolimus)) decreases p(MESH:Proteins, pmod(Ub)) View Subject | View Object

Similar results have recently been observed in vitro using the proteasome inhibitor lactacystin, as pre-treatment with rapamycin attenuates lactacystin-induced apoptosis and reduces lactacystin-induced ubiquitinated protein aggregation [74]. PubMed:18930136

Appears in Networks:

p(HGNC:HDAC6) increases tloc(p(MESH:Proteins, pmod(Ub)), fromLoc(GO:cytoplasm), toLoc(GO:lysosome)) View Subject | View Object

HDAC6 activity appears to be important for trafficking ubiquitinated proteins and lysosomes in vitro and this has led to the suggestion that HDAC6 coordinates delivery of substrates to autophagic machinery [64,70,78]. PubMed:18930136

Appears in Networks:

p(HGNC:SQSTM1) increases deg(p(MESH:Proteins, pmod(Ub))) View Subject | View Object

Thus, it has been suggested that p62 provides a key link between autophagy and the UPS by facilitating autophagic degradation of ubiquitinated proteins. PubMed:18930136

Appears in Networks:

Out-Edges 2

p(MESH:Proteins, pmod(Ub)) increases deg(p(MESH:Proteins, pmod(Ub))) View Subject | View Object

Third, there is ligation of Ub with an epsilon-amino group of lysine in the target protein by an E3 ligase. E3 ligase binds both the target protein and the E2–Ub complex; thousands of substrate- specific E3s ensure selective protein tagging and degradation. PubMed:22908190

Appears in Networks:

p(MESH:Proteins, pmod(Ub)) increases complex(a(GO:"proteasome regulatory particle"), p(MESH:Proteins, pmod(Ub))) View Subject | View Object

Ubiquitinated target proteins bind to the 19S cap (RP), which has a Ub binding site and ATPase activity, and this leads to cleavage of Ub moieties from the target by deubiquitinating enzymes, unfolds the polypeptides and sends them to the narrow channel of the 20S core particle. PubMed:22908190

Appears in Networks:

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If you find BEL Commons useful in your work, please consider citing: Hoyt, C. T., Domingo-Fernández, D., & Hofmann-Apitius, M. (2018). BEL Commons: an environment for exploration and analysis of networks encoded in Biological Expression Language. Database, 2018(3), 1–11.