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p(HGNC:HSPA5)

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

Entity

Name
HSPA5
Namespace
hgnc
Namespace Version
20180906
Namespace URL
https://raw.githubusercontent.com/pharmacome/terminology/b46b65c3da259b6e86026514dfececab7c22a11b/external/hgnc-names.belns

Appears in Networks 4

Chaperoning α7 neuronal nicotinic acetylcholine receptors v1.0.0

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

Molecular chaperones and proteostasis regulation during redox imbalance v1.0.0

Heme Curation v0.0.1-dev

Mechanistic knowledge surrounding heme

In-Edges 4

complex(p(HGNC:HSPA5), p(HGNC:PRNP)) hasComponent p(HGNC:HSPA5) View Subject | View Object

Appears in Networks:

bp(GO:"response to endoplasmic reticulum stress") increases act(p(HGNC:HSPA5)) View Subject | View Object

Upon ER proteotoxic stress, GRP78 dissociates from its binding partners, which are then free to trigger the Unfolded Protein Response (UPR) by regulating specific gene responses aiming to restore ER proteome stability. PubMed:24563850

Appears in Networks:

a(CHEBI:heme) increases p(HGNC:HSPA5) View Subject | View Object

However, in the presence of 40 μM heme, the toxic response was characterized by the strong induction of heat shock proteins, namely HSP70 (HSPA1B, HSPA4, HSPA5, DNAJB1), HSP72 (HSPA1A), HSP105 (HSPH1), and HSP10 (HSPE1), as well as the proteasome adaptor protein sequestosome. PubMed:26794659

Appears in Networks:
Annotations
Cell Ontology (CL)
epithelial cell
MeSH
Kidney
Text Location
Results

p(HGNC:HBB) increases p(HGNC:HSPA5) View Subject | View Object

Immunofluorescence confirmed that renal Hb exposure triggered overexpression of HMOX1 and the unfolded protein response (UPR) chaperone HSP70 in tubule epithelial cells (Figure 2d). PubMed:26794659

Appears in Networks:
Annotations
Cell Ontology (CL)
epithelial cell
MeSH
Kidney
Text Location
Results

Out-Edges 1

p(HGNC:HSPA5) increases p(FPLX:CHRN) View Subject | View Object

There is evidence that AChR folding, assembly and trafficking are influenced by several chaperone proteins, such as the 14-3-3 protein [92,93], BiP [94–96] or calnexin [97–99]. PubMed:22040696

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.