background:
With the presence of the J domain defining a protein as a member, the DnaJ family has evolved with diverse cellular localization and functions and is one of the largest chaperone families. DnaJ heat-shock-induced proteins are derived from the bacterium Escherichia coli and are controlled by the htpR regulatory protein. DnaJ proteins play a critical role in the HSP 70 chaperone machine by interacting with HSP 70 to stimulate ATP hydrolysis. Members of this family contain cysteine-rich regions composed of zinc fingers that form a peptide-binding domain responsible for chaperone function. DnaJ proteins are important mediators of proteolysis and are involved in the regulation of protein degradation, exocytosis and endocytosis. DNAJC21 (DnaJ homolog subfamily C member 21), also known as DNAJA5 or JJJ1, is a 531 amino acid protein that contains two C2H2-type zinc fingers and one J domain. Expressed in placenta, pancreas, kidney and brain, DNAJC21 may be a co-chaperone for HSP 70.
Function:
May act as a co-chaperone for HSP70.
Tissue Specificity:
Brain, placenta, kidney and pancreas.
Similarity:
Contains 2 C2H2-type zinc fingers.
Contains 1 J domain.
Database links:
Entrez Gene: 134218 Human
SwissProt: Q5F1R6 Human
Unigene: 131887 Human
Important Note:
This product as supplied is intended for research use only, not for use in human, therapeutic or diagnostic applications.
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