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Molecular cloning and complete cDNA sequence of UBH1 in mouse testis
Kwang-Hyun Baek1, Kyu-Hyung Park, Yong-Soo Kim
1College of Medicine, Pochon CHA University, Cell and Gene Therapy Research Institute, CHA General Hospital, Seoul, South Korea. baek@cha.ac.kr
Abstract:
We have identified a full-length mouse UBH1 cDNA, encoding a putative deubiquitinating enzyme, from the testis by RT-PCR using primers prepared from sequences conserved amongst deubiquitinating enzymes. Sequence analysis predicts that the UBH1 cDNA encodes a 355 amino acid polypeptide with the molecular weight of approximately 39 kDa containing the highly conserved Cys, Asp, and His domains characteristic of the ubiquitin-specific processing proteases. Biochemical assay revealed that the mouse UBH1 has deubiquitinating enzyme activity and sequence analysis showed 98.3% amino acid identity with human UBH1.