The DnaJ family is one of the largest of all the chaperone families and has evolved with diverse cellular localization and functions. The presence of the J domain defines a protein as a member of the DnaJ family. DnaJ heat shock induced proteins are from the bacterium Escherichia coli and are under the control of the htpR regulatory protein. The DnaJ proteins play a critical role in the HSP 70 chaperone machine by interacting with HSP 70 to stimulate ATP hydrolysis. The proteins contain cysteine rich regions that are composed of zinc fingers that form a peptide binding domain responsible for the chaperone function. DnaJ proteins are important mediators of proteolysis and are involved in the regulation of protein degradation, exocytosis and endocytosis. DnaJB2 (DnaJ homolog subfamily B member 2), also known as HSJ1 or HSPF3, is expressed almost exclusively in the brain, with the highest levels in the frontal cortex and hippocampus. Two isoforms are produced due to alternative splicing.
Tissue Specificity:
Brain (neuronal layers). Weakly, in skeletal muscle and spleen.
Similarity:
Contains 1 J domain.
Contains 2 UIM (ubiquitin-interacting motif) repeats.
SWISS:
P25686
Gene ID:
3300
Database links:
Entrez Gene: 533668 Cow
Entrez Gene: 3300 Human
Entrez Gene: 56812 Mouse
Entrez Gene: 689593 Rat
Omim: 604139 Human
SwissProt: P25686 Human
SwissProt: Q9QYI5 Mouse
Unigene: 77768 Human
Unigene: 40780 Rat
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