UniProt Summary: Probable chaperone. Stimulates ATP hydrolysis and the folding of unfolded proteins mediated by HSPA1A/B (in vitro) (PubMed:24318877). {ECO:0000269|PubMed:24318877}.
Pfam DomainsGO Terms
Pfam Domains
DnaJ C
DnaJ
GO Terms
ATPase activator activity
chaperone cofactor-dependent protein refolding
de novo posttranslational protein folding
de novo protein folding
positive regulation of ATPase activity
chaperone-mediated protein folding
regulation of ATPase activity
chaperone binding
response to heat
unfolded protein binding
response to unfolded protein
response to temperature stimulus
response to topologically incorrect protein
protein folding
positive regulation of hydrolase activity
negative regulation of transcription by RNA polymerase II
response to abiotic stimulus
negative regulation of transcription, DNA-templated
negative regulation of nucleic acid-templated transcription
negative regulation of RNA biosynthetic process
regulation of hydrolase activity
negative regulation of RNA metabolic process
negative regulation of cellular macromolecule biosynthetic process
positive regulation of catalytic activity
negative regulation of nucleobase-containing compound metabolic process
negative regulation of macromolecule biosynthetic process
negative regulation of cellular biosynthetic process
negative regulation of biosynthetic process
negative regulation of gene expression
positive regulation of molecular function
CRISPR Data
Compound HitMost Correlated Genes in ChemogenomicsTissues where Essential in the Avana Dataset (DepMap 20Q1)