[HTML][HTML] Cloning and characterization of mouse UBPy, a deubiquitinating enzyme that interacts with the Ras guanine nucleotide exchange factor CDC25Mm/Ras …
N Gnesutta, M Ceriani, M Innocenti, I Mauri… - Journal of Biological …, 2001 - ASBMB
We used yeast" two-hybrid" screening to isolate cDNA-encoding proteins interacting with the
N-terminal domain of the Ras nucleotide exchange factor CDC25 Mm. Three independent
overlapping clones were isolated from a mouse embryo cDNA library. The full-length cDNA
was cloned by RACE-polymerase chain reaction. It encodes a large protein (1080 amino
acids) highly homologous to the human deubiquitinating enzyme hUBPy and contains a well
conserved domain typical of ubiquitin isopeptidases. Therefore we called this new protein …
N-terminal domain of the Ras nucleotide exchange factor CDC25 Mm. Three independent
overlapping clones were isolated from a mouse embryo cDNA library. The full-length cDNA
was cloned by RACE-polymerase chain reaction. It encodes a large protein (1080 amino
acids) highly homologous to the human deubiquitinating enzyme hUBPy and contains a well
conserved domain typical of ubiquitin isopeptidases. Therefore we called this new protein …
