Molecular cloning and complete cDNA sequence of UBH1 in mouse testis.
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.
Baek
Kwang-Hyun
KH
College of Medicine, Pochon CHA University, Cell and Gene Therapy Research Institute, CHA General Hospital, Seoul, South Korea. baek@cha.ac.kr
Park
Kyu-Hyung
KH
Kim
Yong-Soo
YS
Kim
Myung-Sun
MS
Choi
Hee-Kyung
HK
D000595:Amino Acid Sequence; D000818:Animals; D001483:Base Sequence; D003001:Cloning, Molecular; D018076:DNA, Complementary; D010450:Endopeptidases / Q000235:genetics* / Q000378:metabolism; D006801:Humans; D015151:Immunoblotting; D008297:Male; D051379:Mice; D008969:Molecular Sequence Data; D016415:Sequence Alignment; D013737:Testis / Q000378:metabolism*; D043222:Ubiquitin Thiolesterase
D018076:DNA, Complementary; D010450:Endopeptidases; D043222:Ubiquitin Thiolesterase; C486401:Usp12 protein, mouse