Other names published for CDC31: DSK1, YOR257W
CDC31 LITERATURE TOPICS
- Curated Literature
- Genetics/Cell Biology
- Nucleic Acid Information
- Gene Product Information
- Related Genes/Proteins
- Research Aids
- Genome-wide Analysis
- Proteome-wide Analysis
- Other Topics
- Additional Information
CDC31 - Protein-protein Interactions (20)
| Reference | Other Genes Addressed |
|---|---|
| Bloom J, et al. (2011) Global analysis of cdc14 phosphatase reveals diverse roles in mitotic processes. J Biol Chem 286(7):5434-45 | |
| Araki Y, et al. (2010) N-terminal regions of Mps1 kinase determine functional bifurcation. J Cell Biol 189(1):41-56 | |
| Ellisdon AM, et al. (2010) Structural basis for the interaction between yeast Spt-Ada-Gcn5 acetyltransferase (SAGA) complex components Sgf11 and Sus1. J Biol Chem 285(6):3850-6 | |
| Jani D, et al. (2009) Sus1, Cdc31, and the Sac3 CID region form a conserved interaction platform that promotes nuclear pore association and mRNA export. Mol Cell 33(6):727-37 | |
| Klockner C, et al. (2009) Mutational Uncoupling of the Role of Sus1 in Nuclear Pore Complex Targeting of an mRNA Export Complex and Histone H2B Deubiquitination. J Biol Chem 284(18):12049-56 | |
| Chekanova JA, et al. (2008) Sus1, Sac3, and Thp1 mediate post-transcriptional tethering of active genes to the nuclear rim as well as to non-nascent mRNP. RNA 14(1):66-77 | |
| Chen L and Madura K (2008) Centrin/Cdc31 is a novel regulator of protein degradation. Mol Cell Biol 28(5):1829-40 | |
| Kohler A, et al. (2008) Yeast Ataxin-7 links histone deubiquitination with gene gating and mRNA export. Nat Cell Biol 10(6):707-15 | |
| Oeffinger M, et al. (2007) Comprehensive analysis of diverse ribonucleoprotein complexes. Nat Methods 4(11):951-6 | |
| Kohler A, et al. (2006) The mRNA export factor Sus1 is involved in Spt/Ada/Gcn5 acetyltransferase-mediated H2B deubiquitinylation through its interaction with Ubp8 and Sgf11. Mol Biol Cell 17(10):4228-36 | |
| Li S, et al. (2006) Structural role of Sfi1p-centrin filaments in budding yeast spindle pole body duplication. J Cell Biol 173(6):867-77 | |
| Niepel M, et al. (2005) The nuclear pore complex-associated protein, Mlp2p, binds to the yeast spindle pole body and promotes its efficient assembly. J Cell Biol 170(2):225-35 | |
| Fischer T, et al. (2004) Yeast centrin Cdc31 is linked to the nuclear mRNA export machinery. Nat Cell Biol 6(9):840-8 | |
| Kilmartin JV (2003) Sfi1p has conserved centrin-binding sites and an essential function in budding yeast spindle pole body duplication. J Cell Biol 162(7):1211-21 | |
| Jaspersen SL, et al. (2002) Mps3p is a novel component of the yeast spindle pole body that interacts with the yeast centrin homologue Cdc31p. J Cell Biol 159(6):945-56 | |
| Ivanovska I and Rose MD (2001) Fine structure analysis of the yeast centrin, Cdc31p, identifies residues specific for cell morphology and spindle pole body duplication. Genetics 157(2):503-18 | |
| Sullivan DS, et al. (1998) The yeast centrin, cdc31p, and the interacting protein kinase, Kic1p, are required for cell integrity. J Cell Biol 143(3):751-65 | |
| Geier BM, et al. (1996) Binding of centrins and yeast calmodulin to synthetic peptides corresponding to binding sites in the spindle pole body components Kar1p and Spc110p. J Biol Chem 271(45):28366-74 | |
| Spang A, et al. (1995) The Cdc31p-binding protein Kar1p is a component of the half bridge of the yeast spindle pole body. J Cell Biol 128(5):863-77 | |
| Biggins S and Rose MD (1994) Direct interaction between yeast spindle pole body components: Kar1p is required for Cdc31p localization to the spindle pole body. J Cell Biol 125(4):843-52 |




