Dnlz Gene Summary [Mouse]
Predicted to enable protein folding chaperone and protein-folding chaperone binding activity. Predicted to be involved in several processes, including chaperone-mediated protein complex assembly; protein import into mitochondrial matrix; and protein stabilization. Located in mitochondrion. Orthologous to human DNLZ (DNL-type zinc finger). [provided by Alliance of Genome Resources, Jul 2025]
Details
| Type | Processed Transcript |
| Official Symbol | Dnlz |
| Official Name | DNL-type zinc finger [Source:MGI Symbol;Acc:MGI:106559] |
| Ensembl ID | ENSMUSG00000075467 |
| Bio databases IDs | |
| Aliases | DNL-type zinc finger |
| Synonyms | 1110034G11Rik, bA413M3.2, C9orf151, D2Bwg1335e, DNL-type zinc finger, HEP, HEP1, RGD1308635, TIMM15, ZIM17 |
| Species | Mouse, Mus musculus |
| Orthologies |
Protein Domains
A protein domain is a distinct structural or functional region within a protein that can evolve, function, and exist independently of the rest of the protein chain. These domains in mouse Dnlz often fold into stable, three-dimensional structures and are associated with specific biological functions, such as binding to DNA, other proteins, or small molecules.
- DNL zinc finger
Subcellular Expression
Locations within the cell where the protein is known or predicted to be active, providing insight into its function and cellular context.
- Cytoplasm
- Nucleus
- Mitochondria
- cytosol
- nucleoplasm
Gene Ontology Annotations
Describes the biological processes, cellular components, and molecular functions associated with the mouse Dnlz gene, providing context for its role in the cell.
Biological Process
Functions and activities the gene product is involved in
- protein import into mitochondrial matrix
- chaperone-mediated protein complex assembly
- protein stabilization
- protein folding
Cellular Component
Where in the cell the gene product is active
- nucleus
- mitochondrion
- cytosol
- nucleoplasm
Molecular Function
What the gene product does at the molecular level
- zinc ion binding
- protein binding involved in protein folding
- chaperone binding