Korean J Clin Pathol.
1997 Feb;17(1):190-199.
Cloning of Novel Ubiquitin Conjugating Enzyme Gene(UBC-dp)
Abstract
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BACKGROUND: A major pathway for protein degradation in eukaryocytes is ubiquitin-dependent. A novel species of plant and mammalian E2 homologous to yeast UBC4/UBC5 is involved in polyubiquitination and degradation of off and many other proteins as well.
METHODS
By sequencing the Expressed Sequence Taqs(ESTs) of human dermal papilla cDNA library, we isolated a clone, named K183 which showed high homology to the yeast UBC4/UBC5. We designated this gene as UBC-dp.
RESULTS
K183 clone is 1,222 nucleotides long, and has a coding region of 622 nucleotides and a 3' noncoding region of 538 nucleotides. The presumed open reading frame starting at the 5' terminus of UBC-dp encodes 207 amino acids. The amino acid sequence deduced from the open reading frame of UBC-dp shares 81%, 80% and 80% identities with that of HSUBCH5. yeast UBC4 and yeast UBC5, respectively. The transcripts were ubiquitously expressed in a variety of human tissues. The levels of transcript were relatively high in those tissues such as skeletal muscle, heart, testis and ovary.
CONCLUSIONS
Homology search result suggests that K183 clone is human homolog of the UBC4 and UBC5 which are involved in p53 degradation so its function related with p53 should be studied.
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