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A recently identified protein, termed carboxyl terminus of hsc70-interacting protein (CHIP), has been shown to interact both with the constitutive form of hsc70 and the stress inducible form, hsp70. This novel 35 kDa cytoplasmic protein has been shown to be highly expressed in striated muscle in vivo. Additional studies have shown that this protein is expressed over a broad range of cultured tissues. Through immunoprecipitation experiments, CHIP has been shown to directly bind to the carboxyl terminus of hsc70 and hsp70 where it decreases ATPase activity and reduces overall chaperone efficiency. CHIP has also been identified as an important protein in the ubiquitin-proteasome system. CHIP contains a U-box domain and acts as an E3 ubiquitin-ligase in conjunction with hsc70 and hsp90.
0610033N24Rik; 2210017D18Rik; 2310040B03Rik; Antigen NY-CO-7; AW046544; Carboxy terminus of Hsp70-interacting protein; CHIP; CLL-associated antigen KW-8; E3 ubiquitin-protein ligase CHIP; heat shock protein A binding protein 2 (c-terminal); HSPABP2; LA16c-313D11.6; NY-CO-7; PP1131; RING-type E3 ubiquitin transferase CHIP; SCAR16; SDCCAG7; serologically defined colon cancer antigen 7; STIP1 homology and U box-containing protein 1; STIP1 homology and U-box containing protein 1; STIP1 homology and U-box containing protein 1, E3 ubiquitin protein ligase; Stub1; UBOX1
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