YOL103W-A Physical and Genetic Interactions Help

This page lists genes/proteins that interact with YOL103W-A. See help for information about interaction data.

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Interactions for YOL103W-A (12)
Feature Gene Description Experiment Type Type Action Source Annotation Type Modification Phenotype Note Reference
YGL180W ATG1 Protein kinase required for vesicle formation in autophagy and CVT Biochemical Activity physical interactions Bait BioGRID high-throughput Phosphorylation 32P incorporation on protein chip Ptacek J, et al. (2005) Global analysis of protein phosphorylation in yeast. Nature 438(7068):679-84
YHR115C DMA1 Ubiquitin-protein ligase (E3) Affinity Capture-MS physical interactions Bait BioGRID high-throughput Graumann J, et al. (2004) Applicability of tandem affinity purification MudPIT to pathway proteomics in yeast. Mol Cell Proteomics 3(3):226-37
YBL016W FUS3 Mitogen-activated serine/threonine protein kinase involved in mating Biochemical Activity physical interactions Bait BioGRID high-throughput Phosphorylation 32P incorporation on protein chip Ptacek J, et al. (2005) Global analysis of protein phosphorylation in yeast. Nature 438(7068):679-84
YHR079C IRE1 Serine-threonine kinase and endoribonuclease Biochemical Activity physical interactions Bait BioGRID high-throughput Phosphorylation 32P incorporation on protein chip Ptacek J, et al. (2005) Global analysis of protein phosphorylation in yeast. Nature 438(7068):679-84
YHR082C KSP1 Serine/threonine protein kinase Biochemical Activity physical interactions Bait BioGRID high-throughput Phosphorylation 32P incorporation on protein chip Ptacek J, et al. (2005) Global analysis of protein phosphorylation in yeast. Nature 438(7068):679-84
YGL122C NAB2 Nuclear polyadenylated RNA-binding protein Affinity Capture-RNA physical interactions Bait BioGRID high-throughput High Throughput: The experiment involved high-throughput sequencing of the RNAs that co-precipitated with TAP-tagged Nab2 (Nab2-TAP) Batisse J, et al. (2009) Purification of nuclear poly(A)-binding protein Nab2 reveals association with the yeast transcriptome and a messenger ribonucleoprotein core structure. J Biol Chem 284(50):34911-7
YDL106C PHO2 Homeobox transcription factor Affinity Capture-MS physical interactions Bait BioGRID high-throughput Graumann J, et al. (2004) Applicability of tandem affinity purification MudPIT to pathway proteomics in yeast. Mol Cell Proteomics 3(3):226-37
YPL031C PHO85 Cyclin-dependent kinase Biochemical Activity physical interactions Bait BioGRID high-throughput Phosphorylation 32P incorporation on protein chip Ptacek J, et al. (2005) Global analysis of protein phosphorylation in yeast. Nature 438(7068):679-84
YFR004W RPN11 Metalloprotease subunit of the 19S regulatory particle of the 26S pro Affinity Capture-MS physical interactions Bait BioGRID high-throughput Proteasome interacting proteins (PIPs) were identified using QTAX (quantitative analysis of tandem affinity purified in vivo cross-linked (X) protein complexes) Kaake RM, et al. (2010) Characterization of cell cycle specific protein interaction networks of the yeast 26S proteasome complex by the QTAX strategy. J Proteome Res 9(4):2016-29
YER125W RSP5 E3 ubiquitin ligase of the NEDD4 family Protein-peptide physical interactions Bait BioGRID high-throughput A protein microarray was probed with the third WW domain from RSP5 (YER125W_WW3) Hesselberth JR, et al. (2006) Comparative analysis of Saccharomyces cerevisiae WW domains and their interacting proteins. Genome Biol 7(4):R30
YHR135C YCK1 Palmitoylated plasma membrane-bound casein kinase I isoform Biochemical Activity physical interactions Bait BioGRID high-throughput Phosphorylation 32P incorporation on protein chip Ptacek J, et al. (2005) Global analysis of protein phosphorylation in yeast. Nature 438(7068):679-84
YNL154C YCK2 Palmitoylated plasma membrane-bound casein kinase I isoform Biochemical Activity physical interactions Bait BioGRID high-throughput Phosphorylation 32P incorporation on protein chip Ptacek J, et al. (2005) Global analysis of protein phosphorylation in yeast. Nature 438(7068):679-84