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Publication Abstract from PubMed

Recent studies have shown that ubiquitination is an essential factor in endosomal sorting and virus assembly. The human TSG101 gene has been demonstrated to belong to a group of genes coding for apparently inactive E2 ubiquitin-conjugating enzymes, which exert regulatory effects on E2 activity in cellular ubiquitination processes. In this study, a novel human cDNA (UEV3) encoding a putative protein of 379 amino acids was isolated from a human placenta library that may represent a partial paralogue of human TSG101. The predicted protein contains an N-terminal domain homologous to the catalytic domain of ubiquitin-conjugating enzymes (Ubc), which is fused to a sequence showing significant homology to members of the lactate dehydrogenase protein family. The UEV3 gene is located on chromosome 11 closely adjacent to TSG101 and LDH-C. Northern blot and UEV3-specific reverse transcription/polymerase chain reaction (RT/PCR) analyses of various colon carcinoma cell lines as well as both normal and tumor samples from colon revealed an expression of the UEV3 cDNA in all tested samples.

Identification and characterization of UEV3, a human cDNA with similarities to inactive E2 ubiquitin-conjugating enzymes.,Kloor M, Bork P, Duwe A, Klaes R, von Knebel Doeberitz M, Ridder R Biochim Biophys Acta. 2002 Dec 12;1579(2-3):219-24. PMID:12427560^[2]

From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.