HSPA5
Gene Ontology Biological Process
- ER overload response [IDA]
- activation of signaling protein activity involved in unfolded protein response [IMP]
- cellular response to glucose starvation [ISO]
- cellular response to interleukin-4 [IDA]
- cerebellar Purkinje cell layer development [IMP]
- cerebellum structural organization [IMP]
- maintenance of protein localization in endoplasmic reticulum [ISO]
- negative regulation of apoptotic process [ISO]
- negative regulation of transforming growth factor beta receptor signaling pathway [IGI]
- positive regulation of cell migration [ISO]
- positive regulation of embryonic development [TAS]
- positive regulation of protein ubiquitination [IMP]
- proteolysis involved in cellular protein catabolic process [IDA]
- response to endoplasmic reticulum stress [ISO]
- toxin transport [IMP]
Gene Ontology Molecular Function
Gene Ontology Cellular Component
- COP9 signalosome [ISO]
- cell surface [IDA]
- endoplasmic reticulum [IDA, ISO]
- endoplasmic reticulum chaperone complex [ISO]
- endoplasmic reticulum lumen [IDA]
- endoplasmic reticulum membrane [IDA]
- endoplasmic reticulum-Golgi intermediate compartment [IDA, ISO]
- extracellular vesicular exosome [ISO]
- focal adhesion [ISO]
- integral component of endoplasmic reticulum membrane [ISO]
- membrane [ISO]
- midbody [ISO]
- mitochondrion [ISO]
- myelin sheath [IDA]
- nucleus [ISO]
- plasma membrane [IDA]
- smooth endoplasmic reticulum [ISO]
PDIA4
Gene Ontology Biological Process
Gene Ontology Molecular Function
Gene Ontology Cellular Component
Co-purification
An interaction is inferred from the identification of two or more protein subunits in a purified protein complex, as obtained by classical biochemical fractionation or affinity purification and one or more additional fractionation steps.
Publication
A subset of chaperones and folding enzymes form multiprotein complexes in endoplasmic reticulum to bind nascent proteins.
We demonstrate the existence of a large endoplasmic reticulum (ER)-localized multiprotein complex that is comprised of the molecular chaperones BiP; GRP94; CaBP1; protein disulfide isomerase (PDI); ERdj3, a recently identified ER Hsp40 cochaperone; cyclophilin B; ERp72; GRP170; UDP-glucosyltransferase; and SDF2-L1. This complex is associated with unassembled, incompletely folded immunoglobulin heavy chains. Except for ERdj3, and to a lesser extent PDI, ... [more]
Throughput
- Low Throughput
Related interactions
| Interaction | Experimental Evidence Code | Dataset | Throughput | Score | Curated By | Notes |
|---|---|---|---|---|---|---|
| PDIA4 HSPA5 | Co-fractionation Co-fractionation Interaction inferred from the presence of two or more protein subunits in a partially purified protein preparation. If co-fractionation is demonstrated between 3 or more proteins, then add them as a complex. | High | 0.908 | BioGRID | 2670103 |
Curated By
- BioGRID