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p(HGNC:PTGES3)

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

Entity

Name
PTGES3
Namespace
hgnc
Namespace Version
20180906
Namespace URL
https://raw.githubusercontent.com/pharmacome/terminology/b46b65c3da259b6e86026514dfececab7c22a11b/external/hgnc-names.belns

Appears in Networks 4

A Quantitative Chaperone Interaction Network Reveals the Architecture of Cellular Protein Homeostasis Pathways v1.0.0

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

Imbalances in the Hsp90 Chaperone Machinery: Implications for Tauopathies v1.0.0

TAU and Interaction Partners v1.2.5

TAU Interactions Section of NESTOR

In-Edges 5

complex(p(FPLX:HSP90), p(HGNC:PTGES3)) hasComponent p(HGNC:PTGES3) View Subject | View Object

Appears in Networks:

complex(a(MESH:"Argonaute Proteins"), p(HGNC:PTGES3)) hasComponent p(HGNC:PTGES3) View Subject | View Object

Appears in Networks:

bp(MESH:Aging) decreases p(HGNC:PTGES3) View Subject | View Object

For instance, CyP40, FKBP52, PP5, Hop, p23, and Aha1 are all repressed in the aged brain. PubMed:29311797

Appears in Networks:
Annotations
MeSH
Brain

complex(p(FPLX:HSP90), p(HGNC:FKBP4), p(HGNC:PTGES3), p(HGNC:STIP1)) hasComponent p(HGNC:PTGES3) View Subject | View Object

Appears in Networks:

complex(p(HGNC:MAPT), p(HGNC:PTGES3)) hasComponent p(HGNC:PTGES3) View Subject | View Object

Appears in Networks:

Out-Edges 6

p(HGNC:PTGES3) increases complex(a(MESH:"Protein Kinases"), p(FPLX:HSP90)) View Subject | View Object

For example, the co-chaperones cdc37, a peptidyl-prolyl cis-trans isomerase (PPIase) family member, and p23 are all critical for the transfer of kinases to Hsp90 and maturation of the active protein [76,105] PubMed:21882945

Appears in Networks:

p(HGNC:PTGES3) decreases act(p(FPLX:HSP90), ma(GO:"ATPase activity")) View Subject | View Object

p23 has an opposing effect on Hsp90 compared to Aha1. p23 works by inhibiting the ATPase activity of Hsp90. PubMed:29311797

Appears in Networks:

p(HGNC:PTGES3) decreases path(MESH:"Protein Aggregation, Pathological") View Subject | View Object

As a co-chaperone, p23 works to suppress protein aggregation and exhibits chaperoning activity, although p23 is not able to refold proteins on its own (Freeman et al., 1996). PubMed:29311797

Appears in Networks:

p(HGNC:PTGES3) increases p(HGNC:MAPT) View Subject | View Object

Inhibition of p23 in an siRNA screen of Hsp90 co-chaperones showed that silencing p23 reduced both total and phospho-tau (Jinwal et al., 2012, 2013). PubMed:29311797

Appears in Networks:

p(HGNC:PTGES3) increases p(HGNC:MAPT, pmod(Ph)) View Subject | View Object

Inhibition of p23 in an siRNA screen of Hsp90 co-chaperones showed that silencing p23 reduced both total and phospho-tau (Jinwal et al., 2012, 2013). PubMed:29311797

Appears in Networks:

p(HGNC:PTGES3) decreases bp(GO:"cell death in response to oxidative stress") View Subject | View Object

p23 also plays an important role in preventing endoplasmic reticulum (ER) stress-induced cell death, which can be triggered by misfolded proteins, like tau (Rao et al., 2006; Abisambra et al., 2013). PubMed:29311797

Appears in Networks:

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.