pubmed-article:10089880 | rdf:type | pubmed:Citation | lld:pubmed |
pubmed-article:10089880 | lifeskim:mentions | umls-concept:C0084133 | lld:lifeskim |
pubmed-article:10089880 | lifeskim:mentions | umls-concept:C0084913 | lld:lifeskim |
pubmed-article:10089880 | lifeskim:mentions | umls-concept:C0542341 | lld:lifeskim |
pubmed-article:10089880 | lifeskim:mentions | umls-concept:C0012899 | lld:lifeskim |
pubmed-article:10089880 | lifeskim:mentions | umls-concept:C1524075 | lld:lifeskim |
pubmed-article:10089880 | lifeskim:mentions | umls-concept:C1879748 | lld:lifeskim |
pubmed-article:10089880 | lifeskim:mentions | umls-concept:C1706853 | lld:lifeskim |
pubmed-article:10089880 | lifeskim:mentions | umls-concept:C0679622 | lld:lifeskim |
pubmed-article:10089880 | lifeskim:mentions | umls-concept:C0205314 | lld:lifeskim |
pubmed-article:10089880 | pubmed:issue | 5 | lld:pubmed |
pubmed-article:10089880 | pubmed:dateCreated | 1999-4-22 | lld:pubmed |
pubmed-article:10089880 | pubmed:abstractText | Ubiquitin-conjugating enzyme variant (UEV) proteins resemble ubiquitin-conjugating enzymes (E2s) but lack the defining E2 active-site residue. The MMS2-encoded UEV protein has been genetically implicated in error-free postreplicative DNA repair in Saccharomyces cerevisiae. We show that Mms2p forms a specific heteromeric complex with the UBC13-encoded E2 and is required for the Ubc13p-dependent assembly of polyubiquitin chains linked through lysine 63. A ubc13 yeast strain is UV sensitive, and single, double, and triple mutants of the UBC13, MMS2, and ubiquitin (ubiK63R) genes display a comparable phenotype. These findings support a model in which an Mms2p/Ubc13p complex assembles novel polyubiquitin chains for signaling in DNA repair, and they suggest that UEV proteins may act to increase diversity and selectivity in ubiquitin conjugation. | lld:pubmed |
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pubmed-article:10089880 | pubmed:language | eng | lld:pubmed |
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pubmed-article:10089880 | pubmed:citationSubset | IM | lld:pubmed |
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pubmed-article:10089880 | pubmed:status | MEDLINE | lld:pubmed |
pubmed-article:10089880 | pubmed:month | Mar | lld:pubmed |
pubmed-article:10089880 | pubmed:issn | 0092-8674 | lld:pubmed |
pubmed-article:10089880 | pubmed:author | pubmed-author:PickartC MCM | lld:pubmed |
pubmed-article:10089880 | pubmed:author | pubmed-author:HofmannR MRM | lld:pubmed |
pubmed-article:10089880 | pubmed:issnType | Print | lld:pubmed |
pubmed-article:10089880 | pubmed:day | 5 | lld:pubmed |
pubmed-article:10089880 | pubmed:volume | 96 | lld:pubmed |
pubmed-article:10089880 | pubmed:owner | NLM | lld:pubmed |
pubmed-article:10089880 | pubmed:authorsComplete | Y | lld:pubmed |
pubmed-article:10089880 | pubmed:pagination | 645-53 | lld:pubmed |
pubmed-article:10089880 | pubmed:dateRevised | 2009-11-19 | lld:pubmed |
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pubmed-article:10089880 | pubmed:meshHeading | pubmed-meshheading:10089880... | lld:pubmed |
pubmed-article:10089880 | pubmed:year | 1999 | lld:pubmed |
pubmed-article:10089880 | pubmed:articleTitle | Noncanonical MMS2-encoded ubiquitin-conjugating enzyme functions in assembly of novel polyubiquitin chains for DNA repair. | lld:pubmed |
pubmed-article:10089880 | pubmed:affiliation | Department of Biochemistry, School of Public Health, Johns Hopkins University, Baltimore, Maryland 21205, USA. | lld:pubmed |
pubmed-article:10089880 | pubmed:publicationType | Journal Article | lld:pubmed |
pubmed-article:10089880 | pubmed:publicationType | Research Support, U.S. Gov't, P.H.S. | lld:pubmed |
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