Other names published for SPT23: YKL020C
SPT23 LITERATURE TOPICS
- Curated Literature
- Genetics/Cell Biology
- Nucleic Acid Information
- Gene Product Information
- Protein Processing/Modification/Regulation
- Protein Sequence Features
- Protein-Nucleic Acid Interactions
- Protein-protein Interactions
- Substrates/Ligands/Cofactors
- Related Genes/Proteins
- Research Aids
- Genome-wide Analysis
- Proteome-wide Analysis
- Additional Information
SPT23 - Protein-protein Interactions (8)
| Reference | Other Genes Addressed |
|---|---|
| Miller C, et al. (2011) Dynamic transcriptome analysis measures rates of mRNA synthesis and decay in yeast. Mol Syst Biol 7():458 | |
| Siepe D and Jentsch S (2009) Prolyl isomerase Pin1 acts as a switch to control the degree of substrate ubiquitylation. Nat Cell Biol 11(8):967-72 | |
| Bhattacharya S, et al. (2008) WW domains 2 and 3 of Rsp5p play overlapping roles in binding to the LPKY motif of Spt23p and Mga2p. Int J Biochem Cell Biol 40(1):147-57 | |
| Shcherbik N and Haines DS (2007) Cdc48p(Npl4p/Ufd1p) binds and segregates membrane-anchored/tethered complexes via a polyubiquitin signal present on the anchors. Mol Cell 25(3):385-97 | |
| Rumpf S and Jentsch S (2006) Functional division of substrate processing cofactors of the ubiquitin-selective Cdc48 chaperone. Mol Cell 21(2):261-9 | |
| Shcherbik N, et al. (2004) A single PXY motif located within the carboxyl terminus of Spt23p and Mga2p mediates a physical and functional interaction with ubiquitin ligase Rsp5p. J Biol Chem 279(51):53892-8 | |
| Shcherbik N, et al. (2002) Substrate proteolysis is inhibited by dominant-negative Nedd4 and Rsp5 mutants harboring alterations in WW domain 1. J Cell Sci 115(Pt 5):1041-8 | |
| Rape M, et al. (2001) Mobilization of processed, membrane-tethered SPT23 transcription factor by CDC48(UFD1/NPL4), a ubiquitin-selective chaperone. Cell 107(5):667-77 |



