DNAJC9
Domain
The functional J domain is required for the release from histone-dependent chromatin-binding.
Function
Acts as a dual histone chaperone and heat shock co-chaperone (PubMed:33857403). As a histone chaperone, forms a co-chaperone complex with MCM2 and histone H3-H4 heterodimers; and may thereby assist MCM2 in histone H3-H4 heterodimer recognition and facilitate the assembly of histones into nucleosomes (PubMed:33857403). May also act as a histone co-chaperone together with TONSL (PubMed:33857403). May recruit histone chaperones ASF1A, NASP and SPT2 to histone H3-H4 heterodimers (PubMed:33857403). Also plays a role as co-chaperone of the HSP70 family of molecular chaperone proteins, such as HSPA1A, HSPA1B and HSPA8 (PubMed:17182002, PubMed:33857403). As a co-chaperone, may play a role in the recruitment of HSP70-type molecular chaperone machinery to histone H3-H4 substrates, thereby maintaining the histone structural integrity (PubMed:33857403). Exhibits activity to assemble histones onto DNA in vitro (PubMed:33857403).
Tissue Specificity
Expressed in heart, placenta, liver, skeletal muscle, kidney, pancreas, thymus, ovary, colon and peripheral blood.
Cellular localization
- Nucleus
- Cytoplasm
- Cell membrane
- Predominantly nuclear. Translocates to the cytoplasm and membrane after heat shock.
Alternative names
DnaJ homolog subfamily C member 9, HDJC9, DnaJ protein SB73, DNAJC9