DNAJB2 Proteins

Protein Information

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.

Synonyms

2700059H22Rik; CMT2T; DnaJ (Hsp40) homolog, subfamily B, member 10; DnaJ (Hsp40) homolog, subfamily B, member 2; DnaJ heat shock protein family (Hsp40) member B2; dnaJ homolog subfamily B member 10; DnaJ homolog subfamily B member 2; dnaJ protein homolog 1; Dnajb10; DNAJB2; DSMA5; Heat shock 40 kDa protein 3; heat shock protein J1; heat shock protein, DNAJ-like 1; heat shock protein, neuronal DNAJ-like 1; HSJ1; HSJ-1; HSPF3; mDj8