Annotation inferences using phylogenetic trees
Gene Ontology annotation through association of InterPro records with GO terms
Gene Ontology annotation based on curation of immunofluorescence data
HDJC9, a novel human type C DnaJ/HSP40 member interacts with and cochaperones HSP70 through the J domain.
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HDJC9/DNAJC9 interacts with HSP70s and activates their ATPase activity, both dependent on its J domain, identifying it as a novel HSP70 co-chaperone.
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DNAJC9 is mainly nuclear under normal conditions and translocates to the cytoplasm and plasma membrane upon heat shock via a non-classical lipid-dependent pathway.
Centromere-specific assembly of CENP-a nucleosomes is mediated by HJURP.
Proteomic characterization of the human sperm nucleus.
Proximity biotinylation and affinity purification are complementary approaches for the interactome mapping of chromatin-associated protein complexes.
An AP-MS- and BioID-compatible MAC-tag enables comprehensive mapping of protein interactions and subcellular localizations.
A reference map of the human binary protein interactome.
DNAJC9 integrates heat shock molecular chaperones into the histone chaperone network.
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DNAJC9 is a dual histone H3-H4 chaperone and heat shock co-chaperone; it binds histone H3-H4 substrates in a co-chaperone complex with MCM2.
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DNAJC9 recruits HSP70-type enzymes via its J domain to fold histone H3-H4 substrates during replication- and transcription-coupled nucleosome assembly, integrating ATP-driven folding into the histone supply pathway.
UniProt entry Q8WXX5 (DNJC9_HUMAN), DnaJ homolog subfamily C member 9 / HDJC9