In this study we have cloned a novel member of mouse protein phosphatase 2C family, PP2Cj j, which is composed of 507 amino acids and has a unique N-terminal region. The overall similarity of the amino acid sequence between PP2Cj j and PP2CK K was 22%. On Northern blot analysis PP2Cj j was found to be expressed speci¢cally in the testicular germ cells. PP2Cj j expressed in COS7 cells was able to associate with ubiquitin conjugating enzyme 9 (UBC9) and the association was enhanced by co-expression of small ubiquitin-related modi¢er-1 (SUMO-1), suggesting that PP2Cj j exhibits its speci¢c role through its SUMO-induced recruitment to UBC9. ß
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