Summary of HSPA5
The gene codes for a protein, heat shock protein family A (Hsp70) member 5. It plays a role in monitoring protein transport through the cell [R].
The Function of HSPA5
Probably plays a role in facilitating the assembly of multimeric protein complexes inside the endoplasmic reticulum. Involved in the correct folding of proteins and degradation of misfolded proteins via its interaction with DNAJC10, probably to facilitate the release of DNAJC10 from its substrate.
Protein names
Recommended name:
78 kDa glucose-regulated proteinAlternative name(s):
GRP-78Endoplasmic reticulum lumenal Ca(2+
Heat shock 70 kDa protein 5
Immunoglobulin heavy chain-binding protein
BiP
- RS391957 (HSPA5) ??
- RS430397 (HSPA5) ??
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Top Gene-Substance Interactions
HSPA5 Interacts with These Diseases
Disease | Score |
Substances That Increase HSPA5
Substances | Interaction | Organism | Category |
Substances That Decrease HSPA5
Substances | Interaction | Organism | Category |
Advanced Summary
From UniProt: Autoantigen in rheumatoid arthritis.
From NCBI Gene: The protein encoded by this gene is a member of the heat shock protein 70 (HSP70) family. It is localized in the lumen of the endoplasmic reticulum (ER), and is involved in the folding and assembly of proteins in the ER. As this protein interacts with many ER proteins, it may play a key role in monitoring protein transport through the cell.[provided by RefSeq, Sep 2010] From UniProt: Probably plays a role in facilitating the assembly of multimeric protein complexes inside the endoplasmic reticulum. Involved in the correct folding of proteins and degradation of misfolded proteins via its interaction with DNAJC10, probably to facilitate the release of DNAJC10 from its substrate.
Conditions with Increased Gene Activity
Condition | Change (log2fold) | Comparison | Species | Experimental variables | Experiment name |
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Conditions with Decreased Gene Activity
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Technical
The following transcription factors affect gene expression:
Gene Pathways:
Molecular Function:
- Glycoprotein Binding
- Calcium Ion Binding
- Atp Binding
- Atpase Activity
- Enzyme Binding
- Protein Domain Specific Binding
- Ubiquitin Protein Ligase Binding
- Ribosome Binding
- Unfolded Protein Binding
- Chaperone Binding
- Misfolded Protein Binding
- Cadherin Binding Involved In Cell-Cell Adhesion
Biological Processes:
- Er Overload Response
- Activation Of Signaling Protein Activity Involved In Unfolded Protein Response
- Cerebellum Structural Organization
- Cerebellar Purkinje Cell Layer Development
- Substantia Nigra Development
- Positive Regulation Of Cell Migration
- Er-Associated Ubiquitin-Dependent Protein Catabolic Process
- Negative Regulation Of Transforming Growth Factor Beta Receptor Signaling Pathway
- Endoplasmic Reticulum Unfolded Protein Response
- Positive Regulation Of Protein Ubiquitination
- Protein Folding In Endoplasmic Reticulum
- Maintenance Of Protein Localization In Endoplasmic Reticulum
- Ire1-Mediated Unfolded Protein Response
- Perk-Mediated Unfolded Protein Response
- Atf6-Mediated Unfolded Protein Response
- Cellular Response To Glucose Starvation
- Negative Regulation Of Apoptotic Process
- Regulation Of Protein Folding In Endoplasmic Reticulum
- Cellular Response To Antibiotic
- Cellular Response To Manganese Ion
- Cellular Response To Interleukin-4
- Negative Regulation Of Protein Homodimerization Activity
- Toxin Transport
- Regulation Of Atf6-Mediated Unfolded Protein Response
- Regulation Of Ire1-Mediated Unfolded Protein Response
- Regulation Of Perk-Mediated Unfolded Protein Response
- Positive Regulation Of Transcription From Rna Polymerase Ii Promoter In Response To Endoplasmic Reticulum Stress
Drug Bank:
- Acetylsalicylic Acid
- Antihemophilic Factor (Recombinant)