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DnaJ homolog subfamily C member 9 (DNAJC9)
- Target
- DNAJC9
- Molecular classification
- Heat shock protein, Histone chaperone, Co-chaperone
01
Overview
DnaJ homolog subfamily C member 9 (DNAJC9) is a multifunctional co-chaperone protein that acts as both a heat shock co-chaperone (Hsp40 family) and a histone chaperone. It forms complexes with histone H3–H4 and other factors like MCM2 to promote correct folding of newly synthesized histones. DNAJC9 is essential for replication- and transcription-coupled nucleosome assembly, helping resolve aberrant histone intermediates and protecting chromatin integrity[1][2][3]. It functions as an integrator of ATP-dependent HSP70 enzyme activity—directing chaperone machinery to histones H3–H4 and maintaining their structural integrity during proteostasis processes[1][3]. DNAJC9 is primarily localized to the cytosol and nucleoplasm and plays roles in protein folding, chromatin assembly, and the positive regulation of ATP-dependent processes. Dysregulated DNAJC9 expression has been observed in neuropsychiatric conditions, implicating a broader role in nuclear protein homeostasis and transcriptional regulation[1][2][3].
- Other names
- JDD1HDCJ9SB73DnaJ protein SB73DnaJ (Hsp40) homolog, subfamily C, member 9
02
Biological functions
Chromatin assemblyProtein foldingMaintenance of chromatin integrityPositive regulation of ATP-dependent activityNucleosome assembly
03
Disease associations
Neuropsychiatric disorder (e.g., schizophrenia)Other (rare genetic syndromes such as Joubert syndrome 36, Epithelial recurrent erosion dystrophy)
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