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- W135235169 abstract "All known functions of ubiquitin are mediated through its covalent attachment to other proteins. The post-translational formation of ubiquitin--protein conjugates is preceded by an ATP-requiring step in which the carboxyl terminus of ubiquitin is adenylated and subsequently joined, through a thiolester bond, to a cysteine residue in the ubiquitin-activating enzyme, also known as E1. We report the isolation and functional analysis of the gene (UBA1) for the ubiquitin-activating enzyme of the yeast Saccharomyces cerevisiae. UBA1 encodes a 114 kd protein whose amino acid sequence contains motifs characteristic of nucleotide-binding sites. Expression of catalytically active UBA1 protein in E. coli, which lacks the ubiquitin system, confirmed that the yeast UBA1 gene encodes a ubiquitin-activating enzyme. Deletion of the UBA1 gene is lethal, demonstrating that the formation of ubiquitin--protein conjugates is essential for cell viability." @default.
- W135235169 created "2016-06-24" @default.
- W135235169 creator A5013945577 @default.
- W135235169 creator A5039562263 @default.
- W135235169 creator A5069736026 @default.
- W135235169 date "1991-01-01" @default.
- W135235169 modified "2023-10-18" @default.
- W135235169 title "UBA 1: an essential yeast gene encoding ubiquitin-activating enzyme." @default.
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- W135235169 doi "https://doi.org/10.1002/j.1460-2075.1991.tb07940.x" @default.
- W135235169 hasPubMedCentralId "https://www.ncbi.nlm.nih.gov/pmc/articles/452634" @default.
- W135235169 hasPubMedId "https://pubmed.ncbi.nlm.nih.gov/1989885" @default.
- W135235169 hasPublicationYear "1991" @default.
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