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Dnaja1 - DnaJ heat shock protein family (Hsp40) member A1 (house mouse)

Gene
Symbol
Dates
  • Create:
    2016-09-14
  • Modify:
    2025-01-29
Description
The protein encoded by the Dnaja1 gene is a member of the DnaJ family, whose members act as cochaperones of heat shock protein 70. Heat shock proteins facilitate protein folding, trafficking, prevention of aggregation, and proteolytic degradation. Members of this family are characterized by a highly conserved N-terminal J domain, a glycine/phenylalanine-rich region, four CxxCxGxG zinc finger repeats, and a C-terminal substrate-binding domain. The J domain mediates the interaction with heat shock protein 70 to recruit substrates and regulate ATP hydrolysis activity. Mice deficient for this gene display reduced levels of activation‐induced deaminase, an enzyme that deaminates deoxycytidine at the immunoglobulin genes during immune responses. In addition, mice lacking this gene exhibit severe defects in spermatogenesis. Several pseudogenes of this gene are found on other chromosomes. Alternative splicing results in multiple transcript variants. [provided by RefSeq, Sep 2015]
Predicted to enable several functions, including C3HC4-type RING finger domain binding activity; Hsp70 protein binding activity; and signaling receptor binding activity. Acts upstream of or within androgen receptor signaling pathway; flagellated sperm motility; and spermatogenesis. Predicted to be located in membrane and microtubule cytoskeleton. Predicted to be active in cytosol. Is expressed in several structures, including 1st branchial arch mandibular component; alimentary system; brain; genitourinary system; and hemolymphoid system. Orthologous to human DNAJA1 (DnaJ heat shock protein family (Hsp40) member A1).

1 Names and Identifiers

1.1 Synonyms

  • HSJ-2
  • Hsj2
  • Nedd7
  • dnaJ homolog subfamily A member 1
  • DnaJ (Hsp40) homolog, subfamily A, member 1
  • dnaJ protein homolog 2
  • heat shock 40 kDa protein 4
  • heat shock protein J2
  • heat shock protein, Dnaj-like 2
  • neural precursor cell expressed, developmentally down-regulated gene 7

1.2 Other Identifiers

1.2.1 Ensembl ID

1.2.2 Alliance Gene ID

1.2.3 Bgee Gene ID

1.2.4 MGI ID

1.2.5 VEuPathDB ID

1.2.6 Wikidata

3 Proteins

3.1 Protein Function

Co-chaperone for HSPA8/Hsc70. Plays a role in protein transport into mitochondria via its role as co-chaperone. Stimulates ATP hydrolysis, but not the folding of unfolded proteins mediated by HSPA1A (in vitro). Promotes apoptosis in response to cellular stress mediated by exposure to anisomycin or UV (By similarity). Functions as co-chaperone for HSPA1B and negatively regulates the translocation of BAX from the cytosol to mitochondria in response to cellular stress, thereby protecting cells against apoptosis.

3.2 Protein 3D Structures

3.2.1 AlphaFold Structures

Highly accurate protein structure prediction with AlphaFold. Nature. 2021 Aug;596(7873):583-589. DOI:10.1038/s41586-021-03819-2. PMID:34265844; PMCID:PMC8371605

3.3 Protein Targets

4 BioAssays

4.1 RNAi BioAssays

5 Interactions and Pathways

5.1 Interactions

5.2 Pathways

6 Biochemical Reactions

7 Expression

8 Literature

8.1 Consolidated References

8.2 Gene-Chemical Co-Occurrences in Literature

8.3 Gene-Gene Co-Occurrences in Literature

8.4 Gene-Disease Co-Occurrences in Literature

9 Patents

9.1 Gene-Chemical Co-Occurrences in Patents

9.2 Gene-Gene Co-Occurrences in Patents

9.3 Gene-Disease Co-Occurrences in Patents

10 Classification

10.1 Gene Ontology: Biological Process

10.2 Gene Ontology: Cellular Component

10.3 Gene Ontology: Molecular Function

11 Information Sources

  1. NCBI Gene
    LICENSE
    NCBI Website and Data Usage Policies and Disclaimers
    https://www.ncbi.nlm.nih.gov/home/about/policies/
  2. PubChem
  3. Alliance of Genome Resources
    LICENSE
    All annotations and data produced by Alliance members that are accessible from alliancegenome.org are distributed under a CC BY 4.0 license (https://creativecommons.org/licenses/by/4.0/).
    https://www.alliancegenome.org/privacy-warranty-licensing
  4. BioGRID
    LICENSE
    The MIT License (MIT); Copyright Mike Tyers Lab
    https://wiki.thebiogrid.org/doku.php/terms_and_conditions
  5. Database of Interacting Proteins (DIP)
    LICENSE
    All DIP database records available under the terms set by the Creative Commons Attribution-NoDerivs License.
    https://dip.doe-mbi.ucla.edu/dip/termsofuse.html
  6. STRING: functional protein association networks
  7. Mouse Genome Informatics (MGI)
    LICENSE
    MGI data and annotations are licensed under a Creative Commons Attribution 4.0 International License (CC-BY).
    https://www.informatics.jax.org/mgihome/other/copyright.shtml
  8. NCBI Gene Expression Omnibus (GEO)
  9. Swiss Institute of Bioinformatics Bgee
    LICENSE
    Creative Commons Zero license (CC0)
    https://www.bgee.org/about/
  10. UniProt
    LICENSE
    We have chosen to apply the Creative Commons Attribution (CC BY 4.0, http://creativecommons.org/licenses/by/4.0/) License to all copyrightable parts of our databases.
    https://www.uniprot.org/help/license
  11. VEuPathDB: The Eukaryotic Pathogen, Vector and Host Informatics Resource
    LICENSE
    All data on VEuPathDB websites are provided freely for public use.
    https://veupathdb.org/veupathdb/app/static-content/about.html
  12. Wikidata
  13. Gene Ontology (GO)
    LICENSE
    Gene Ontology Consortium data and data products are licensed under the Creative Commons Attribution 4.0 Unported License (https://creativecommons.org/licenses/by/4.0/legalcode)
    http://geneontology.org/docs/go-citation-policy/
  14. AlphaFold DB
    LICENSE
    All of the data provided is freely available for both academic and commercial use under Creative Commons Attribution 4.0 (CC-BY 4.0) licence terms.
    https://alphafold.ebi.ac.uk/faq
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