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Entity

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

Appears in Networks 5

In-Edges 14

a(MESH:Denervation) increases bp(GO:"protein catabolic process") View Subject | View Object

For example, upregulation of the pathway is observed during massive degradation of skeletal muscle proteins that occurs under normal fasting but also under pathological conditions such as cancer-induced cachexia, severe sepsis, metabolic acidosis, or following denervation PubMed:14556719

path(MESH:Acidosis) increases bp(GO:"protein catabolic process") View Subject | View Object

For example, upregulation of the pathway is observed during massive degradation of skeletal muscle proteins that occurs under normal fasting but also under pathological conditions such as cancer-induced cachexia, severe sepsis, metabolic acidosis, or following denervation PubMed:14556719

path(MESH:Cachexia) increases bp(GO:"protein catabolic process") View Subject | View Object

For example, upregulation of the pathway is observed during massive degradation of skeletal muscle proteins that occurs under normal fasting but also under pathological conditions such as cancer-induced cachexia, severe sepsis, metabolic acidosis, or following denervation PubMed:14556719

path(MESH:Sepsis) increases bp(GO:"protein catabolic process") View Subject | View Object

For example, upregulation of the pathway is observed during massive degradation of skeletal muscle proteins that occurs under normal fasting but also under pathological conditions such as cancer-induced cachexia, severe sepsis, metabolic acidosis, or following denervation PubMed:14556719

complex(a(GO:"proteasome complex"), p(HGNC:UCHL5)) increases bp(GO:"protein catabolic process") View Subject | View Object

It was initially believed that the presence of DUBs at the proteasome (such as Uch37/UchL5 and Usp14) would promote the degradation of proteins through facilitating substrate processing (see also the next section) PubMed:24457024

complex(a(GO:"proteasome complex"), p(HGNC:USP14)) increases bp(GO:"protein catabolic process") View Subject | View Object

It was initially believed that the presence of DUBs at the proteasome (such as Uch37/UchL5 and Usp14) would promote the degradation of proteins through facilitating substrate processing (see also the next section) PubMed:24457024

complex(a(GO:"proteasome complex"), p(HGNC:USP14)) decreases bp(GO:"protein catabolic process") View Subject | View Object

However, recent studies have shown that, by contrast, upon chemical inhibition of the proteasome-bound DUB Usp14, the degradation of aggregation-prone substrates in mammalian tissue culture cells significantly increased [65] PubMed:24457024

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

Alternatively, either Hsp70 or Hsp90 can recruit the ubiquitin E3 ligase, C-terminal Hsp70 interacting protein (CHIP), to degrade the bound substrate [104] PubMed:21882945

p(FPLX:HSP90) increases bp(GO:"protein catabolic process") View Subject | View Object

Although both Hsp70 and Hsp90 can promote degradation of client proteins, it has recently been shown that, functionally, the Hsp70 complex often dominates triage decisions [85,107,109] PubMed:21882945

p(INTERPRO:"Heat shock protein 70 family") increases bp(GO:"protein catabolic process") View Subject | View Object

Although both Hsp70 and Hsp90 can promote degradation of client proteins, it has recently been shown that, functionally, the Hsp70 complex often dominates triage decisions [85,107,109] PubMed:21882945

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

The PN branch of degradation includes the ubiquitin- proteasome system (UPS) and machinery of autophagy (23, 196–200). PubMed:23746257

act(p(FPLX:HSPA)) association bp(GO:"protein catabolic process") View Subject | View Object

Hsp70 chaperones are a ubiquitous class of proteins. They are involved in a wide range of protein quality control functions, including de novo protein folding, refolding of stress- denatured proteins, protein transport, mem- brane translocation, and protein degradation. PubMed:23746257

p(FPLX:Proteasome) increases bp(GO:"protein catabolic process") View Subject | View Object

The PN branch of degradation includes the ubiquitin- proteasome system (UPS) and machinery of autophagy (23, 196–200). PubMed:23746257

bp(GO:"autophagosome-lysosome fusion") increases bp(GO:"protein catabolic process") View Subject | View Object

Once formed, new autophagosomes move through a stepwise maturation process that culminates with fusion to a lysosome permitting degradation of the lumenal contents. PubMed:18930136

Out-Edges 2

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

For example, upregulation of the pathway is observed during massive degradation of skeletal muscle proteins that occurs under normal fasting but also under pathological conditions such as cancer-induced cachexia, severe sepsis, metabolic acidosis, or following denervation PubMed:14556719

bp(GO:"protein catabolic process") association act(p(FPLX:HSPA)) View Subject | View Object

Hsp70 chaperones are a ubiquitous class of proteins. They are involved in a wide range of protein quality control functions, including de novo protein folding, refolding of stress- denatured proteins, protein transport, mem- brane translocation, and protein degradation. PubMed:23746257

About

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.