Molecular cloning, sequence, and tissue distribution of the human ubiquitin-activating enzyme E1

P. M. Handley, M. Mueckler, N. R. Siegel, A. Ciechanover, A. L. Schwartz

Research output: Contribution to journalArticle

103 Scopus citations

Abstract

The ubiquitin-activating enzyme E1 catalyzes the first step in ubiquitin conjugation. We have cloned and sequenced the cDNA for human E1. This clone predicts a protein of 110,450 Da. Cys-194 lies within a region of identity to active-site Cys-88 of the ubiquitin carrier protein E2, suggesting a potential role for this region in enzymatic function of this protein. In addition, Cys-454 lies within a region of identity to the thiol ester consensus sequence of several proteins involved in thioester formation. Tissue distribution reveals a single 3.5-kilobase E1 message ubiquitous among tissues and cell lines.

Original languageEnglish
Pages (from-to)258-262
Number of pages5
JournalProceedings of the National Academy of Sciences of the United States of America
Volume88
Issue number1
DOIs
StatePublished - Jan 17 1991

Keywords

  • protein degradation

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