UniProt UniProt http://www.uniprot.org peggie-2002-1 yeast Saccharomyces cerevisiae Baker's yeast fluorescence imaging fluorescence microscopy fluorescence imaging anti-tag immunocytochemistry anti-tag immunocytochemistry Peggie MW., MacKelvie SH., Bloecher A., Knatko EV., Tatchell K., Stark MJ. m.j.r.stark@dundee.ac.uk Journal of cell science 2002 imex curation Only protein-protein interactions imex curation peggie-2002-2 yeast Saccharomyces cerevisiae Baker's yeast affinity chrom affinity chromatography technology Affinity purification Affinity purification affinity chrom fingerprinting peptide massfingerprinting fingerprinting Peggie MW., MacKelvie SH., Bloecher A., Knatko EV., Tatchell K., Stark MJ. The protein complex was purified on an IgG-Sepharose column then eluted following TEV cleavage of the Protein A tafg. m.j.r.stark@dundee.ac.uk Journal of cell science 2002 imex curation Only protein-protein interactions imex curation peggie-2002-3 yeast Saccharomyces cerevisiae Baker's yeast anti tag coip anti tag coimmunoprecipitation anti tag coip anti tag western anti tag western blot anti tag western Peggie MW., MacKelvie SH., Bloecher A., Knatko EV., Tatchell K., Stark MJ. m.j.r.stark@dundee.ac.uk Journal of cell science 2002 imex curation Only protein-protein interactions imex curation pp12_yeast Serine/threonine-protein phosphatase PP1-2 GLC7 CID1 DIS2 YER133W protein protein yeast Saccharomyces cerevisiae Baker's yeast MDSQPVDVDNIIDRLLEVRGSKPGQQVDLEENEIRYLCSKARSIFIKQPILLELEAPIKICGDIHGQYYDLLRLFEYGGFPPESNYLFLGDYVDRGKQSLETICLLLAYKIKYPENFFILRGNHECASINRIYGFYDECKRRYNIKLWKTFTDCFNCLPIAAIIDEKIFCMHGGLSPDLNSMEQIRRVMRPTDIPDVGLLCDLLWSDPDKDIVGWSENDRGVSFTFGPDVVNRFLQKQDMELICRAHQVVEDGYEFFSKRQLVTLFSAPNYCGEFDNAGAMMSVDESLLCSFQILKPAQKSLPRQAGGRKKK 71B20E3A4ED93235 sds22_yeast Protein phosphatase 1 regulatory subunit SDS22 YKL193C SDS22 EGP1 protein protein yeast Saccharomyces cerevisiae Baker's yeast MDKNSVNKDSEEKDERHKIEVVDDTNPDFITADSELTQDLPDDVEVIDLVHLKIKSLEDLNLYRFKNLKQLCLRQNLIESISEVEVLPHDKIVDLDFYDNKIKHISSNVNKLTKLTSLDLSFNKIKHIKNLENLTDLENLYFVQNSISKIENLSTLKSLKNLELGGNKVHSIEPDSFEGLSNLEEIWLGKNSIPRLINLHPLKNLKILSIQSNKLKKIENLEELTNLEELYLSHNFITKIEGLEKNLKLTTLDVTSNKITSLENLNHLSNLTDIWASFNKIDQSFESLGENLSALSRLETIYLEGNPIQLENKTSYRRKLTMNLPPSLQKIDATYIRG 1EF434C7276ABAEA glc7-sds22-5 3313922 N/A 3313925 unspecified role unspecified role neutral component neutral component n-terminal ha tag ha tag YPYDVPDYA epitope tag YPYDVPDYA epitope tag undetermined undetermined sequence position undetermined undetermined undetermined sequence position undetermined false N/A 3313926 unspecified role unspecified role neutral component neutral component c-terminal myc tag myc tag EUKLISEED epitope tag EUKLISEED epitope tag c-term range C-terminal range c-term range c-term range C-terminal range c-term range false colocalization colocalization false false false Fig. 1 glc7-sds22-6 3313923 N/A 3313925 unspecified role unspecified role prey prey N/A 3313926 unspecified role unspecified role bait bait c-terminal protein a tag protein a tag protein A protein A c-term range C-terminal range c-term range c-term range C-terminal range c-term range false physical association physical association false false false Fig. 2A, 2B Higher molecular weight bands were also observed but not identified. glc7-sds22-7 3313924 N/A 3313925 unspecified role unspecified role prey prey n-terminal ha tag ha tag YPYDVPDYA epitope tag YPYDVPDYA epitope tag n-term range n-terminal range n-term range n-term range n-terminal range n-term range false N/A 3313926 unspecified role unspecified role bait bait c-terminal myc tag myc tag EUKLISEED epitope tag EUKLISEED epitope tag c-term range C-terminal range c-term range c-term range C-terminal range c-term range false P36047:p.[Ile54Thr;Ile193Thr] mutation decreasing strength mutation decreasing interaction strength mutation decreasing strength certain certain sequence position certain certain certain sequence position certain false certain certain sequence position certain certain certain sequence position certain false physical association physical association false false false Fig. 6 The SDS22 Ile54Thr,Ile1932Thr mutations reduced the interaction at 4C, and disrupted it at 30C. The interaction was conformed by immuno-depletion.