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bp(GO:"protein ubiquitination")

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Entity

Name
protein ubiquitination
Namespace
go
Namespace Version
20180921
Namespace URL
https://raw.githubusercontent.com/pharmacome/terminology/b46b65c3da259b6e86026514dfececab7c22a11b/external/go-names.belns

Appears in Networks 7

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

Molecular chaperones and regulation of tau quality control: strategies for drug discovery in tauopathies v1.0.0

Molecular Chaperone Functions in Protein Folding and Proteostasis v1.0.0

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

Pathological missorting of endogenous MAPT/Tau in neurons caused by failure of protein degradation systems v1.0.0

Pathological missorting of endogenous MAPT/Tau in neurons caused by failure of protein degradation systems v1.0.1

In-Edges 19

p(HGNC:UBA3) increases bp(GO:"protein ubiquitination") View Subject | View Object

E3s catalyze the last step in the conjugation process: covalent attachment of ubiquitin to the substrate. PubMed:14556719

Appears in Networks:

p(HGNC:UBA3) increases bp(GO:"protein ubiquitination") View Subject | View Object

In some other cases, the first ubiquitin moiety is conjugated to the substrate by one E3, while chain elongation is catalyzed by a different ligase, often termed E4 PubMed:14556719

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p(HGNC:UCHL1) decreases bp(GO:"protein ubiquitination") View Subject | View Object

It has been reported recently that while the monomeric form of UCH-L1 catalyzes deubiquitination, the dimers display a ubiquitin ligase activity that generates ubiquitin-K63 bonds (Liu et al., 2002). PubMed:14556719

Appears in Networks:

p(HGNC:NFKBIA, pmod(Sumo)) decreases bp(GO:"protein ubiquitination") View Subject | View Object

For example, in the case of IkBalpha,the inhibitor of the transcriptional regulator NF-kB, modification by SUMO-1 was shown to protect the substrate from ubiquitination PubMed:14556719

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complex(a(GO:"proteasome complex"), p(HGNC:BAG6)) increases bp(GO:"protein ubiquitination") View Subject | View Object

Because Bag6 interacts with both E3 ligases as well as the proteasome [57,58,60], it may promote both the ubiquitination and delivery of misfolded proteins to the proteasome while preventing their aggregation PubMed:24457024

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complex(a(MESH:Proteins), a(MESH:Ubiquitin), p(HGNC:UBA2), p(HGNC:UBA3)) increases bp(GO:"protein ubiquitination") View Subject | View Object

Finally, the E3 ubiquitin ligase binds to both the E2-bound ubiquitin and the protein substrate, promoting the transfer of ubiquitin onto the substrate PubMed:24457024

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p(HGNC:UBA2) increases bp(GO:"protein ubiquitination") View Subject | View Object

These studies demonstrated that both E2s and E3s can affect the conformation of the ubiquitin on the E2 surface to promote its transfer to the substrate PubMed:24457024

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p(HGNC:UBA3) increases bp(GO:"protein ubiquitination") View Subject | View Object

However, earlier biochemical investigations on the SCF (Skp, Cullin, F-box containing) ubiquitin ligase complex, the archetypal member of the cullin–RING ligases, indicated that E3s can also positively influence the rate of ubiquitin transfer from the E2 to the protein substrate [17,18]. PubMed:24457024

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p(HGNC:UBA3) increases bp(GO:"protein ubiquitination") View Subject | View Object

These studies demonstrated that both E2s and E3s can affect the conformation of the ubiquitin on the E2 surface to promote its transfer to the substrate PubMed:24457024

Appears in Networks:

p(HGNC:UBA3) increases bp(GO:"protein ubiquitination") View Subject | View Object

Some E3s can also stabilize the conformation between ubiquitin and the E2, thereby accelerating further the rate of conjugation of ubiquitin to proteins PubMed:24457024

Appears in Networks:

complex(p(HGNC:BAG6), p(HGNC:UBA3)) increases bp(GO:"protein ubiquitination") View Subject | View Object

Because Bag6 interacts with both E3 ligases as well as the proteasome [57,58,60], it may promote both the ubiquitination and delivery of misfolded proteins to the proteasome while preventing their aggregation PubMed:24457024

Appears in Networks:

p(HGNC:VCP) increases bp(GO:"protein ubiquitination") View Subject | View Object

Cdc48/p97 generally acts downstream of ubiquitin ligases, although its activity may also promote ubiquitination in some cases; a major challenge is to delineate further the mechanism of action of this multipurpose enzyme PubMed:24457024

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act(p(HGNC:STUB1)) increases bp(GO:"protein ubiquitination") View Subject | View Object

For example, BAG-2 inhibits client ubiquitination by CHIP by interfering with the interaction between CHIP and E2 ubiquitin-conjugating enzymes [148]. PubMed:21882945

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p(HGNC:BAG2) decreases bp(GO:"protein ubiquitination") View Subject | View Object

For example, BAG-2 inhibits client ubiquitination by CHIP by interfering with the interaction between CHIP and E2 ubiquitin-conjugating enzymes [148]. PubMed:21882945

Appears in Networks:

composite(p(FPLX:HSP90), p(FPLX:HSPA), p(HGNC:BAG1), p(HGNC:BAG3), p(HGNC:STUB1)) increases bp(GO:"protein ubiquitination") View Subject | View Object

For example, Hsp70 and Hsp90 cooperate with the U-box-dependent ubiquitin ligase CHIP (C terminus of Hsc70-interacting protein) and a variety of other cofactors (such as BAG1 and BAG3) to ubiquitinate client proteins (23, 86, 198). PubMed:23746257

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p(HGNC:UBA1) increases bp(GO:"protein ubiquitination") View Subject | View Object

This model is consistent with an older study showing that inactivation of the ubiquitin-activating enzyme E1 leads to a defect in autolysosomal degradation and to an absence of ubiquitin-positive proteins within lysosomes [68]. PubMed:18930136

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tloc(p(HGNC:WDFY3), fromLoc(GO:nucleus), toLoc(GO:cytoplasm)) increases bp(GO:"protein ubiquitination") View Subject | View Object

In cells that are exposed to stressors such as starvation or UPS inhibition, Alfy relocalizes from the nuclear envelope to filamentous cytoplasmic structures that are near autophagic membranes and ubiquitinated protein inclusions, as well as within autophagosomes [77]. PubMed:18930136

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a(CHEBI:epoxomicin) increases bp(GO:"protein ubiquitination") View Subject | View Object

Similarly, a dramatic elevation of ubiquitinated substrates (from 4.2±0.1 to 37±1) upon epoxomicin treatment was detected in dendrites containing MAPT (compare Fig. S4E and Fig. S4F). PubMed:30145931

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Annotations
MeSH
Dendrites

composite(a(CHEBI:epoxomicin), p(HGNC:MAPT)) increases bp(GO:"protein ubiquitination") View Subject | View Object

Similarly, a dramatic elevation of ubiquitinated substrates (from 4.2±0.1 to 37±1) upon epoxomicin treatment was detected in dendrites containing MAPT (compare Fig. S4E and Fig. S4F). PubMed:30145931

Appears in Networks:
Annotations
Confidence
Medium
MeSH
Dendrites

Out-Edges 4

bp(GO:"protein ubiquitination") increases bp(GO:"lysosomal protein catabolic process") View Subject | View Object

In many of these cases, the modification leads to targeting of the tagged substrate for degradation in the lysosome/vacuole PubMed:14556719

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bp(GO:"protein ubiquitination") increases bp(GO:"protein catabolic process in the vacuole") View Subject | View Object

In many of these cases, the modification leads to targeting of the tagged substrate for degradation in the lysosome/vacuole PubMed:14556719

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bp(GO:"protein ubiquitination") regulates bp(GO:"proteasome-mediated ubiquitin-dependent protein catabolic process") View Subject | View Object

The UPS can be regulated at the level of ubiquitination or at the level of proteasome activity PubMed:14556719

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bp(GO:"protein ubiquitination") regulates bp(GO:autophagy) View Subject | View Object

The process of autophagy is controlled by parallel activation cascades that involve ubiquitin-like (UBL) protein modification, strikingly similar to the activation cascade that regulates the UPS (Figure 2a). PubMed:18930136

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BEL Commons is developed and maintained in an academic capacity by Charles Tapley Hoyt and Daniel Domingo-Fernández at the Fraunhofer SCAI Department of Bioinformatics with support from the IMI project, AETIONOMY. It is built on top of PyBEL, an open source project. Please feel free to contact us here to give us feedback or report any issues. Also, see our Publishing Notes and Data Protection information.

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.