title: DNAJC17 Gene
category: gene
<div class="infobox infobox-gene"> [@soto2011]
<table> [@jha2018]
<tr><th colspan="2" style="background:#f3e5f5; text-align:center; font-size:1.1em;">DNAJC17</th></tr> [@sweeney2017]
<tr><td><strong>Gene Symbol</strong></td><td>DNAJC17</td></tr> [@jiang2019]
<tr><td><strong>Full Name</strong></td><td>DnaJ Heat Shock Protein Family Member C17</td></tr> [@cox2020]
<tr><td><strong>Chromosomal Location</strong></td><td>15q21.1</td></tr> [@mitra2021]
<tr><td><strong>NCBI Gene ID</strong></td><td>[56126](https://www.ncbi.nlm.nih.gov/gene/56126)</td></tr>
<tr><td><strong>Ensembl ID</strong></td><td>ENSG00000149691</td></tr>
<tr><td><strong>OMIM ID</strong></td><td>[613358](https://www.omim.org/entry/613358)</td></tr>
<tr><td><strong>UniProt ID</strong></td><td>[Q9NWV8](https://www.uniprot.org/uniprot/Q9NWV8)</td></tr>
<tr><td><strong>Protein Length</strong></td><td>304 amino acids</td></tr>
<tr><td><strong>Molecular Weight</strong></td><td>34.5 kDa</td></tr>
<tr>
<td class="label">KG Connections</td>
<td><a href="/atlas" style="color:#4fc3f7">1 edges</a></td>
</tr>
</table>
</div>
title: DNAJC17 Gene
category: gene
<div class="infobox infobox-gene"> [@soto2011]
<table> [@jha2018]
<tr><th colspan="2" style="background:#f3e5f5; text-align:center; font-size:1.1em;">DNAJC17</th></tr> [@sweeney2017]
<tr><td><strong>Gene Symbol</strong></td><td>DNAJC17</td></tr> [@jiang2019]
<tr><td><strong>Full Name</strong></td><td>DnaJ Heat Shock Protein Family Member C17</td></tr> [@cox2020]
<tr><td><strong>Chromosomal Location</strong></td><td>15q21.1</td></tr> [@mitra2021]
<tr><td><strong>NCBI Gene ID</strong></td><td>[56126](https://www.ncbi.nlm.nih.gov/gene/56126)</td></tr>
<tr><td><strong>Ensembl ID</strong></td><td>ENSG00000149691</td></tr>
<tr><td><strong>OMIM ID</strong></td><td>[613358](https://www.omim.org/entry/613358)</td></tr>
<tr><td><strong>UniProt ID</strong></td><td>[Q9NWV8](https://www.uniprot.org/uniprot/Q9NWV8)</td></tr>
<tr><td><strong>Protein Length</strong></td><td>304 amino acids</td></tr>
<tr><td><strong>Molecular Weight</strong></td><td>34.5 kDa</td></tr>
<tr>
<td class="label">KG Connections</td>
<td><a href="/atlas" style="color:#4fc3f7">1 edges</a></td>
</tr>
</table>
</div>
DNAJC17 (DnaJ Heat Shock Protein Family Member C17) is a member of the DNAJ family of co-chaperones, which are characterized by the presence of a conserved J domain that enables them to interact with [Hsp70](/proteins/hsp70-protein) [heat shock proteins](/entities/heat-shock-proteins) and regulate their ATPase activity. DNAJC17 is a Type II DNAJ protein, containing a J domain at the N-terminus followed by a glycine/phenylalanine-rich region and a C-terminal client-binding domain. While DNAJC17 was initially predicted to function as a molecular chaperone, its exact biological roles and disease associations remain an active area of investigation.
The DNAJ protein family (also known as Hsp40 family) consists of over 40 members in humans, categorized into three main classes based on their domain architecture: Type I (DNAJA), Type II (DNAJB), and Type III (DNAJC). DNAJC17 represents a relatively uncharacterized member of this family, with emerging evidence suggesting roles in [protein quality control](/mechanisms/protein-quality-control-network)mechanisms/protein-quality-control-network), [RNA processing](/mechanisms/rna-processing), and potentially in [neurodegenerative disease](/diseases/alzheimers-disease) contexts.
The DNAJC17 gene is located on chromosome 15q21.1, spanning approximately 8.5 kilobases of genomic DNA. The gene consists of 9 exons encoding a 304-amino acid protein. The gene structure is relatively simple compared to other DNAJ family members, with a compact architecture reflecting its specialized function.
DNAJC17 exhibits broad but specific expression patterns across human tissues:
DNAJC17 localizes primarily to the [cytoplasm](/cellular-structures/cytoplasm), where it can interact with its Hsp70 partners. Some studies suggest additional localization to the [nucleus](/cellular-structures/nucleus), particularly in association with RNA processing compartments. The protein may also associate with [mitochondria](/mechanisms/mitochondrial-dysfunction-neurodegeneration) in certain cell types.
DNAJC17 contains several functional domains:
While DNAJC17 remains incompletely characterized, several molecular functions have been proposed:
Chaperone Activity: As a DNAJ co-chaperone, DNAJC17 likely assists Hsp70 in protein folding, refolding, and clearance of misfolded proteins. The J domain couples substrate delivery to Hsp70 ATP hydrolysis.
Protein Quality Control: DNAJC17 may participate in the cellular protein quality control network, helping to target damaged or aggregation-prone proteins for refolding or degradation via the [proteasome](/proteins/proteasome-20s) or [autophagy](/mechanisms/autophagy) pathways.
RNA Processing: Some evidence suggests DNAJ proteins can associate with RNA-protein complexes, potentially linking protein quality control to RNA metabolism.
While direct evidence linking DNAJC17 to [Alzheimer's disease (AD)](/diseases/alzheimers-disease) is limited, several indirect connections suggest potential involvement:
Similar considerations apply to [Parkinson's disease (PD)](/diseases/parkinsons-disease):
[ALS](/diseases/amyotrophic-lateral-sclerosis) involves aggregation of [TDP-43](/mechanisms/tdp-43-proteinopathy), FUS, and SOD1 proteins. DNAJ proteins may influence the handling of these disease proteins.
DNAJC17 primarily interacts with cytosolic Hsp70 proteins:
While specific client proteins for DNAJC17 are not well established, the protein may handle:
DNAJC17 participates in several cellular pathways:
While DNAJC17 is not currently a therapeutic target, understanding its function may provide insights into:
DNAJC17 is a member of the DNAJ/Hsp40 co-chaperone family with predicted roles in protein quality control and potentially in RNA processing. While its exact functions remain under investigation, DNAJC17 participates in Hsp70-mediated protein folding and clearance pathways relevant to neurodegenerative diseases. Further research is needed to fully characterize DNAJC17's biological roles and therapeutic potential in conditions like [Alzheimer's](/diseases/alzheimers-disease), [Parkinson's](/diseases/parkinsons-disease-disease), and ALS.