IntAct European Bioinformatics Institute IntAct intact http://www.ebi.ac.uk/ http://www.ebi.ac.uk/intact/query/${ac} EBI-[0-9]+|IA:[0-9]+ INTerAction database (IntAct) provides an open source database and toolkit for the storage, presentation and analysis of molecular interactions. http://www.ebi.ac.uk/intact European Bioinformatics Institute; Wellcome Trust Genome Campus; Hinxton, Cambridge; CB10 1SD; United Kingdom http://www.ebi.ac.uk/intact/ Systematic functional prioritization of protein posttranslational modifications. Systematic functional prioritization of protein posttranslational modifications. Cell (0092-8674) 2012 imex curation Beltrao P., Albanèse V., Kenner L.R., Swaney D.L., Burlingame A., Villén J., Lim W.A., Fraser J.S., Frydman J., Krogan N.J. Interaction between proteins fused to the two fragments (f1 and f2) of a split cytosine deaminase allows it to fold and become enzymatically active. The folded cytosine deaminase converts cytosine to uracil, permitting growth on –Ura media, but also converts 5-FC to 5-FUTP, which kills cells on media containing 5-FC. In contrast, when the cytosine deaminase fragments are fused to proteins that do not interact, growth is no longer supported on –Ura media, but the strain is viable on media containing 5-FC. pedro.beltrao@ucsf.edu, krogan@cmp.ucsf.edu, pbeltrao@ebi.ac.uk 13-Jan-2014: Contacted by IntAct-Help. Only protein-protein interactions yeasx Saccharomyces cerevisiae (Baker's yeast) Baker's yeast anti tag coip anti tag coimmunoprecipitation anti tag coip anti tag western anti tag western blot anti tag western Beltrao P., Albanèse V., Kenner L.R., Swaney D.L., Burlingame A., Villén J., Lim W.A., Fraser J.S., Frydman J., Krogan N.J. Interaction between proteins fused to the two fragments (f1 and f2) of a split cytosine deaminase allows it to fold and become enzymatically active. The folded cytosine deaminase converts cytosine to uracil, permitting growth on –Ura media, but also converts 5-FC to 5-FUTP, which kills cells on media containing 5-FC. In contrast, when the cytosine deaminase fragments are fused to proteins that do not interact, growth is no longer supported on –Ura media, but the strain is viable on media containing 5-FC. pedro.beltrao@ucsf.edu, krogan@cmp.ucsf.edu, pbeltrao@ebi.ac.uk Accepted 2013-DEC-04 by ORCHARD Cell (0092-8674) 2012 Only protein-protein interactions imex curation Systematic functional prioritization of protein posttranslational modifications. Systematic functional prioritization of protein posttranslational modifications. Cell (0092-8674) 2012 imex curation Beltrao P., Albanèse V., Kenner L.R., Swaney D.L., Burlingame A., Villén J., Lim W.A., Fraser J.S., Frydman J., Krogan N.J. Interaction between proteins fused to the two fragments (f1 and f2) of a split cytosine deaminase allows it to fold and become enzymatically active. The folded cytosine deaminase converts cytosine to uracil, permitting growth on –Ura media, but also converts 5-FC to 5-FUTP, which kills cells on media containing 5-FC. In contrast, when the cytosine deaminase fragments are fused to proteins that do not interact, growth is no longer supported on –Ura media, but the strain is viable on media containing 5-FC. pedro.beltrao@ucsf.edu, krogan@cmp.ucsf.edu, pbeltrao@ebi.ac.uk 13-Jan-2014: Contacted by IntAct-Help. Only protein-protein interactions yeasx Saccharomyces cerevisiae (Baker's yeast) Baker's yeast complementation protein complementation assay PCA complementation predetermined predetermined participant predetermined Beltrao P., Albanèse V., Kenner L.R., Swaney D.L., Burlingame A., Villén J., Lim W.A., Fraser J.S., Frydman J., Krogan N.J. Interaction between proteins fused to the two fragments (f1 and f2) of a split cytosine deaminase allows it to fold and become enzymatically active. The folded cytosine deaminase converts cytosine to uracil, permitting growth on –Ura media, but also converts 5-FC to 5-FUTP, which kills cells on media containing 5-FC. In contrast, when the cytosine deaminase fragments are fused to proteins that do not interact, growth is no longer supported on –Ura media, but the strain is viable on media containing 5-FC. pedro.beltrao@ucsf.edu, krogan@cmp.ucsf.edu, pbeltrao@ebi.ac.uk Accepted 2013-DEC-04 by ORCHARD Cell (0092-8674) 2012 Only protein-protein interactions imex curation met30_yeast F-box protein MET30 YIL046W MET30 Methionine-requiring protein 30 E3 ubiquitin ligase complex SCF(Met30) subunit MET30 protein protein yeast Saccharomyces cerevisiae Baker's yeast MRRERQRMMSFEDKDKDDLDNSNSNNSSEMTDTAMMPPLKRLLITGSSDDLAQGSSGKKKMTMATRSPSSSPDLATNDSGTRVQPLPEYNFTKFCYRHNPDIQFSPTHTACYKQDLKRTQEINANIAKLPLQEQSDIHHIISKYSNSNDKIRKLILDGILSTSCFPQLSYISSLVTHMIKIDFISILPQELSLKILSYLDCQSLCNATRVCRKWQKLADDDRVWYHMCEQHIDRKCPNCGWGLPLLHMKRARIQQNSTGSSSNADIQTQTTRPWKVIYRERFKVESNWRKGHCRIQEFKGHMDGVLTLQFNYRLLFTGSYDSTIGIWDLFTGKLIRRLSGHSDGVKTLYFDDRKLITGSLDKTIRVWNYITGECISTYRGHSDSVLSVDSYQKVIVSGSADKTVKVWHVESRTCYTLRGHTEWVNCVKLHPKSFSCFSCSDDTTIRMWDIRTNSCLKVFRGHVGQVQKIIPLTIKDVENLATDNTSDGSSPQDDPTMTDGADESDTPSNEQETVLDENIPYPTHLLSCGLDNTIKLWDVKTGKCIRTQFGHVEGVWDIAADNFRIISGSHDGSIKVWDLQSGKCMHTFNGRRLQRETQHTQTQSLGDKVAPIACVCIGDSECFSGDEFGCVKMYKFDLND 5135D4BCA2E1EB97 5135D4BCA2E1EB97 skp1_yeast Suppressor of kinetochore protein 1 SKP1 CBF3D YDR328C D9798.14 Centromere DNA-binding protein complex CBF3 subunit D E3 ubiquitin ligase complex SCF subunit SKP1 protein protein yeast Saccharomyces cerevisiae Baker's yeast MVTSNVVLVSGEGERFTVDKKIAERSLLLKNYLNDMHDSNLQNNSDSESDSDSETNHKSKDNNNGDDDDEDDDEIVMPVPNVRSSVLQKVIEWAEHHRDSNFPDEDDDDSRKSAPVDSWDREFLKVDQEMLYEIILAANYLNIKPLLDAGCKVVAEMIRGRSPEEIRRTFNIVNDFTPEEEAAIRRENEWAEDR 746DDE6470A69432 746DDE6470A69432 met30-skp1-1 2 4 unspecified role unspecified role neutral component neutral component f1 cytosine fragment tag tag undetermined undetermined sequence position undetermined undetermined undetermined sequence position undetermined P52286:p.Ser162Asp mutation decreasing mutation decreasing interaction hotspot hotspot mutation decreasing certain certain sequence position certain certain certain sequence position certain S D Wed May 02 14:40:45 BST 2018 This feature has been corrected as a result of our quality control procedures. The original label was 'ser162asp' Tue Jun 30 17:50:59 BST 2020 This feature has been corrected as a result of our quality control procedures. The original label was 'p.Ser162Asp' This mutation mimics a phosphorylation in the ser162 site. 3 unspecified role unspecified role neutral component neutral component f2 cytosine fragment tag tag undetermined undetermined sequence position undetermined undetermined undetermined sequence position undetermined physical association physical association 3d skp1-met30 1 4 unspecified role unspecified role bait bait P52286:p.Ser162Asp mutation mutation certain certain sequence position certain certain certain sequence position certain S D Wed May 02 18:40:00 BST 2018 This feature has been corrected as a result of our quality control procedures. The original label was 'ser162asp' Tue Jun 30 19:25:24 BST 2020 This feature has been corrected as a result of our quality control procedures. The original label was 'p.Ser162Asp' This mutation mimics a phosphorylation in the ser162 site. region flag tag flag tag FLAG-tagged FLAG DYKDDDDKV epitope tag DYKDDDDKV epitope tag FLAG FLAG-tagged undetermined undetermined sequence position undetermined undetermined undetermined sequence position undetermined 3 unspecified role unspecified role prey prey region myc tag myc tag EUKLISEED epitope tag EUKLISEED epitope tag undetermined undetermined sequence position undetermined undetermined undetermined sequence position undetermined physical association physical association 3f This interaction is reduced in comparison with the one involving the Skp1-S162A mutant. skp1-met30-1 1 4 unspecified role unspecified role bait bait P52286:p.Ser162Ala mutation mutation certain certain sequence position certain certain certain sequence position certain S A Wed May 02 18:52:55 BST 2018 This feature has been corrected as a result of our quality control procedures. The original label was 'ser162ala' Tue Jun 30 18:39:09 BST 2020 This feature has been corrected as a result of our quality control procedures. The original label was 'p.Ser162Ala' region flag tag flag tag FLAG-tagged FLAG DYKDDDDKV epitope tag DYKDDDDKV epitope tag FLAG FLAG-tagged undetermined undetermined sequence position undetermined undetermined undetermined sequence position undetermined 3 unspecified role unspecified role prey prey region myc tag myc tag EUKLISEED epitope tag EUKLISEED epitope tag undetermined undetermined sequence position undetermined undetermined undetermined sequence position undetermined physical association physical association 3f