HSPA5
HSPA5 (Endoplasmic reticulum chaperone BiP) is an enzyme. The public catalogues list it as a drug target and a biomarker, and clinical evidence ties its variants to diagnosis, prognosis or drug response. Tied to Colorectal cancer.
Overview
Endoplasmic reticulum chaperone that plays a key role in protein folding and quality control in the endoplasmic reticulum lumen. Involved in the correct folding of proteins and degradation of misfolded proteins via its interaction with DNAJC10/ERdj5, probably to facilitate the release of DNAJC10/ERdj5 from its substrate. Acts as a key repressor of the EIF2AK3/PERK and ERN1/IRE1-mediated unfolded protein response (UPR).
CIViC holds 1 clinical evidence item and 0 assertions across 1 variant, naming Fluorouracil.
- Target · the protein and the cell it sits on
- Drug · antibody, small molecule, cell or radioligand
- Effect · signal, damage or kill
In plain words · HSPA5 (Endoplasmic reticulum chaperone BiP) is an enzyme. The public catalogues list it as a drug target and a biomarker, and clinical evidence ties its variants to diagnosis, prognosis or drug response. Tied to Colorectal cancer.
- 1 · What it is
HSPA5 (Endoplasmic reticulum chaperone BiP) is an enzyme. The public catalogues list it as a drug target and a biomarker, and clinical evidence ties its variants to diagnosis, prognosis or drug response. Tied to Colorectal cancer.
- 2 · What goes wrong in cancer
Endoplasmic reticulum chaperone that plays a key role in protein folding and quality control in the endoplasmic reticulum lumen.
- 3 · How drugs use it
No product in this corpus aims at HSPA5 yet. Inhibitors are shaped to fit the enzyme's active site so the reaction the cancer relies on stops.
External identifiers
Sources: HGNC HGNC:5238 (approved symbol, name, aliases, locus and cross-references (hgnc_complete_set.txt)); UniProt P11021 (protein name, function text, keywords and locations (REST API)); CIViC gene HSPA5 (1 evidence items, 0 assertions, 1 variants; diseases: Colorectal Cancer (GraphQL API, CC0))
Biology
Endoplasmic reticulum chaperone that plays a key role in protein folding and quality control in the endoplasmic reticulum lumen. Involved in the correct folding of proteins and degradation of misfolded proteins via its interaction with DNAJC10/ERdj5, probably to facilitate the release of DNAJC10/ERdj5 from its substrate. Acts as a key repressor of the EIF2AK3/PERK and ERN1/IRE1-mediated unfolded protein response (UPR). In the unstressed endoplasmic reticulum, recruited by DNAJB9/ERdj4 to the luminal region of ERN1/IRE1, leading to disrupt the dimerisation of ERN1/IRE1, thereby inactivating ERN1/IRE1. Also binds and inactivates EIF2AK3/PERK in unstressed cells. Accumulation of misfolded protein in the endoplasmic reticulum causes release of HSPA5/BiP from ERN1/IRE1 and EIF2AK3/PERK, allowing their homodimerisation and subsequent activation. Location: Endoplasmic reticulum lumen; Melanosome; Cytoplasm; Cell surface (UniProt). Locus 9q33.3 (HGNC).
- Colorectal cancer: CIViC evidence names this disease
Notes
top- Written by scripts/fetch-cancer-genes.ts from CIViC, Open Targets, IntOGen, HGNC and UniProt; the function text is UniProt's, condensed and in UK spelling. Roles: CIViC lists 1 therapies; CIViC holds 1 clinical evidence items on its variants. Evidence tier "clinical-evidence" is the strongest of those signals.
- Prevalence not recorded: none of the sources gives a positivity rate.
Latest papers
topQuery for this target: (TITLE:"HSPA5" OR ABSTRACT:"HSPA5" OR TITLE:"heat shock protein family A Hsp70 member 5" OR ABSTRACT:"heat shock protein family A Hsp70 member 5" OR TITLE:"Endoplasmic reticulum chaperone BiP" OR ABSTRACT:"Endoplasmic reticulum chaperone BiP" OR TITLE:"BiP" OR ABSTRACT:"BiP" OR TITLE:"GRP78" OR ABSTRACT:"GRP78") AND (cancer OR tumor OR tumour OR oncology OR carcinoma OR lymphoma OR leukemia OR leukaemia OR myeloma OR sarcoma OR melanoma OR glioma). Results are unfiltered search hits about HSPA5, not a curated reading list.