Description
Product Characteristics:
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. DnaJA2 (DnaJ homolog subfamily A member 2), also known as HIRA-interacting protein 4 or cell cycle progression restoration gene 3 protein, contains one CR-type zinc finger and is a co-chaperone of HSC 70.
Subcellular location: Cell membrane
Synonyms: Cell cycle progression 3 protein, Cell cycle progression restoration gene 3 protein, CPR 3, CPR3, Dj3, DJA 2, DJA2, DnaJ Hsp40 homolog subfamily A member 2, DNAJ, DnaJ homolog subfamily A member 2, DNAJA 2, Dnaja2, DNJ 3, Dnj3, DNJA2_HUMAN, HIRA interacting protein 4, HIRA-interacting protein 4, HIRIP 4, HIRIP4, OTTHUMP00000164136, PRO3015, RDJ 2, RDJ2, Renal carcinoma antigen NY REN 14, Renal carcinoma antigen NY-REN-14.
Target Information: The protein encoded by this gene belongs to the evolutionarily conserved DNAJ/HSP40 family of proteins, which regulate molecular chaperone activity by stimulating ATPase activity. DNAJ proteins may have up to 3 distinct domains: a conserved 70-amino acid J domain, usually at the N terminus\, a glycine/phenylalanine (G/F)-rich region\, and a cysteine-rich domain containing 4 motifs resembling a zinc finger domain. The product of this gene works as a cochaperone of Hsp70s in protein folding and mitochondrial protein import in vitro. [provided by RefSeq, Jul 2008]