DIP Database of Interacting Proteins 611 Young Drive East; Los Angeles CA 90095; USA http://dip.doe-mbi.ucla.edu/ dip@mbi.ucla.edu Cooperative structure of the heterotrimeric pre-mRNA retention and splicing complex. Cooperative structure of the heterotrimeric pre-mRNA retention and splicing complex. Nature structural & molecular biology 2014 imex curation Wysoczański P., Schneider C., Xiang S., Munari F., Trowitzsch S., Wahl MC., Lührmann R., Becker S., Zweckstetter M. Only protein-protein interactions in vitro In vitro peptide array peptide array predetermined predetermined participant predetermined Wysoczański P., Schneider C., Xiang S., Munari F., Trowitzsch S., Wahl MC., Lührmann R., Becker S., Zweckstetter M. DIP original experiment: DIP-262213X Nature structural & molecular biology 2014 IMEx Cooperative structure of the heterotrimeric pre-mRNA retention and splicing complex. Cooperative structure of the heterotrimeric pre-mRNA retention and splicing complex. Cooperative structure of the heterotrimeric pre-mRNA retention and splicing complex. Nature structural & molecular biology 2014 imex curation Wysoczański P., Schneider C., Xiang S., Munari F., Trowitzsch S., Wahl MC., Lührmann R., Becker S., Zweckstetter M. Only protein-protein interactions in vitro In vitro peptide array peptide array predetermined predetermined participant predetermined Wysoczański P., Schneider C., Xiang S., Munari F., Trowitzsch S., Wahl MC., Lührmann R., Becker S., Zweckstetter M. DIP original experiment: DIP-262212X Nature structural & molecular biology 2014 IMEx Cooperative structure of the heterotrimeric pre-mRNA retention and splicing complex. Cooperative structure of the heterotrimeric pre-mRNA retention and splicing complex. Cooperative structure of the heterotrimeric pre-mRNA retention and splicing complex. Nature structural & molecular biology 2014 imex curation Wysoczański P., Schneider C., Xiang S., Munari F., Trowitzsch S., Wahl MC., Lührmann R., Becker S., Zweckstetter M. Only protein-protein interactions in vitro In vitro nmr nuclear magnetic resonance NMR NMR nmr predetermined predetermined participant predetermined Wysoczański P., Schneider C., Xiang S., Munari F., Trowitzsch S., Wahl MC., Lührmann R., Becker S., Zweckstetter M. DIP original experiment: DIP-262209X Nature structural & molecular biology 2014 IMEx Cooperative structure of the heterotrimeric pre-mRNA retention and splicing complex. Cooperative structure of the heterotrimeric pre-mRNA retention and splicing complex. Cooperative structure of the heterotrimeric pre-mRNA retention and splicing complex. Nature structural & molecular biology 2014 imex curation Wysoczański P., Schneider C., Xiang S., Munari F., Trowitzsch S., Wahl MC., Lührmann R., Becker S., Zweckstetter M. Only protein-protein interactions in vitro In vitro itc isothermal titration calorimetry ITC ITC itc predetermined predetermined participant predetermined Wysoczański P., Schneider C., Xiang S., Munari F., Trowitzsch S., Wahl MC., Lührmann R., Becker S., Zweckstetter M. DIP original experiment: DIP-262210X Nature structural & molecular biology 2014 IMEx Cooperative structure of the heterotrimeric pre-mRNA retention and splicing complex. Cooperative structure of the heterotrimeric pre-mRNA retention and splicing complex. Cooperative structure of the heterotrimeric pre-mRNA retention and splicing complex. Nature structural & molecular biology 2014 imex curation Wysoczański P., Schneider C., Xiang S., Munari F., Trowitzsch S., Wahl MC., Lührmann R., Becker S., Zweckstetter M. Only protein-protein interactions in vitro In vitro nmr nuclear magnetic resonance NMR NMR nmr predetermined predetermined participant predetermined Wysoczański P., Schneider C., Xiang S., Munari F., Trowitzsch S., Wahl MC., Lührmann R., Becker S., Zweckstetter M. DIP original experiment: DIP-262207X Nature structural & molecular biology 2014 IMEx Cooperative structure of the heterotrimeric pre-mRNA retention and splicing complex. Cooperative structure of the heterotrimeric pre-mRNA retention and splicing complex. Cooperative structure of the heterotrimeric pre-mRNA retention and splicing complex. Nature structural & molecular biology 2014 imex curation Wysoczański P., Schneider C., Xiang S., Munari F., Trowitzsch S., Wahl MC., Lührmann R., Becker S., Zweckstetter M. Only protein-protein interactions in vitro In vitro itc isothermal titration calorimetry ITC ITC itc predetermined predetermined participant predetermined Wysoczański P., Schneider C., Xiang S., Munari F., Trowitzsch S., Wahl MC., Lührmann R., Becker S., Zweckstetter M. DIP original experiment: DIP-262211X Nature structural & molecular biology 2014 IMEx Cooperative structure of the heterotrimeric pre-mRNA retention and splicing complex. Cooperative structure of the heterotrimeric pre-mRNA retention and splicing complex. Cooperative structure of the heterotrimeric pre-mRNA retention and splicing complex. Nature structural & molecular biology 2014 imex curation Wysoczański P., Schneider C., Xiang S., Munari F., Trowitzsch S., Wahl MC., Lührmann R., Becker S., Zweckstetter M. Only protein-protein interactions in vitro In vitro nmr nuclear magnetic resonance NMR NMR nmr predetermined predetermined participant predetermined Wysoczański P., Schneider C., Xiang S., Munari F., Trowitzsch S., Wahl MC., Lührmann R., Becker S., Zweckstetter M. DIP original experiment: DIP-262208X Nature structural & molecular biology 2014 IMEx Cooperative structure of the heterotrimeric pre-mRNA retention and splicing complex. pml1_yeast Pre-mRNA leakage protein 1 L1591 YLR016C PML1 protein protein yeast Saccharomyces cerevisiae Baker's yeast MFHRRKRPYNTRNYGHDDKKFKSQYIDIMPDFSPSGLLELESNNKEGIALKHVEPQDAISPDNYMDMLGLEARDRTMYELVIYRKNDKDKGPWKRYDLNGRSCYLVGRELGHSLDTDLDDRTEIVVADIGIPEETSSKQHCVIQFRNVRGILKCYVMDLDSSNGTCLNNVVIPGARYIELRSGDVLTLSEFEEDNDYELIFMNV DA39B4465EFFD378 DA39B4465EFFD378 ist3_yeast U2 snRNP component IST3 IST3 SNU17 YIR005W YIB5W U2 snRNP protein SNU17 Increased sodium tolerance protein 3 protein protein yeast Saccharomyces cerevisiae Baker's yeast MNKIQQINDKELQSGILSPHQSWHNEYKDNAYIYIGNLNRELTEGDILTVFSEYGVPVDVILSRDENTGESQGFAYLKYEDQRSTILAVDNLNGFKIGGRALKIDHTFYRPKRSLQKYYEAVKEELDRDIVSKNNAEKLILAKKDQPN 9D51C3043AB823D2 9D51C3043AB823D2 cwc26_yeast Pre-mRNA-splicing factor CWC26 YGL174W G1642 BUD13 SLC7 Complexed with CEF1 protein 26 Bud site selection protein 13 Synthetic lethal with CLF1 protein 7 CWC26 protein protein yeast Saccharomyces cerevisiae Baker's yeast MALHQYLSETYGPTKPKNKTKKKKKESKSDANSDKTSLIVKERLSTLQQEQEKSGVASFSKFDKQKSKNIWKNLETNELSHAITHPSASSITGNESKNDLKEIRAQEPLVTVADKSKTRKTIYRDAQGHKIQEDSKIDDSSFSRSKYEDEKAAEREQYLKNLNMGDVQKLGINVDAHDKKKNQTASSLTIEDPAITFTHDKERTVKTSLLGRKLYDKPAPENRFAIMPGSRWDGVHRSNGFEEKWFAKQNEINEKKVQSYTLQEDY 1584B390121325CD 1584B390121325CD bud13p-snu17p-1 2 10 unspecified role unspecified role bait bait Region 215-245 Region 215-245 sufficient to bind sufficient binding region sufficient to bind certain certain sequence position certain certain certain sequence position certain in vitro In vitro 9 unspecified role unspecified role prey prey Region 25-138 Region 25-138 sufficient to bind sufficient binding region sufficient to bind certain certain sequence position certain certain certain sequence position certain GST-tag GST-tag gst tag glutathione s tranferase tag glutathione S-tranferase tag glutathione S-tranferase tag gst tag n-term range n-terminal range n-term range n-term range n-terminal range n-term range ecolx Escherichia coli direct interaction direct interaction bud13p-pml1p-1 5 10 unspecified role unspecified role unspecified role unspecified role Region 215-245 Region 215-245 sufficient to bind sufficient binding region sufficient to bind certain certain sequence position certain certain certain sequence position certain ecolx Escherichia coli 8 unspecified role unspecified role unspecified role unspecified role Region 22-42 Region 22-42 sufficient to bind sufficient binding region sufficient to bind certain certain sequence position certain certain certain sequence position certain ecolx Escherichia coli 9 unspecified role unspecified role unspecified role unspecified role Region 25-138 Region 25-138 sufficient to bind sufficient binding region sufficient to bind certain certain sequence position certain certain certain sequence position certain ecolx Escherichia coli physical association physical association pml1p-snu17p-1 3 8 unspecified role unspecified role unspecified role unspecified role Region 22-42 Region 22-42 sufficient to bind sufficient binding region sufficient to bind certain certain sequence position certain certain certain sequence position certain ecolx Escherichia coli 9 unspecified role unspecified role unspecified role unspecified role Region 25-138 Region 25-138 sufficient to bind sufficient binding region sufficient to bind certain certain sequence position certain certain certain sequence position certain ecolx Escherichia coli direct interaction direct interaction pml1p-snu17p-2 1 8 unspecified role unspecified role bait bait Region 22-42 Region 22-42 sufficient to bind sufficient binding region sufficient to bind certain certain sequence position certain certain certain sequence position certain in vitro In vitro 9 unspecified role unspecified role prey prey Region 25-138 Region 25-138 sufficient to bind sufficient binding region sufficient to bind certain certain sequence position certain certain certain sequence position certain GST-tag GST-tag gst tag glutathione s tranferase tag glutathione S-tranferase tag glutathione S-tranferase tag gst tag n-term range n-terminal range n-term range n-term range n-terminal range n-term range ecolx Escherichia coli direct interaction direct interaction pml1p-snu17p-3 6 8 unspecified role unspecified role unspecified role unspecified role Region 22-42 Region 22-42 sufficient to bind sufficient binding region sufficient to bind certain certain sequence position certain certain certain sequence position certain Q07930:p.Phe32Ala F32A mutation disrupting strength mutation disrupting interaction strength mutation disrupting strength alanine scanning alanine scanning certain certain sequence position certain certain certain sequence position certain F A This feature has been corrected as a result of our quality control procedures. The original label was 'F32A'. Wed May 02 14:50:30 BST 2018 This feature has been corrected as a result of our quality control procedures. The original label was 'phe32ala' Tue Jun 30 17:26:19 BST 2020 This feature has been corrected as a result of our quality control procedures. The original label was 'p.Phe32Ala' Q07930:p.Leu38Ala L38A mutation decreasing strength mutation decreasing interaction strength mutation decreasing strength alanine scanning alanine scanning certain certain sequence position certain certain certain sequence position certain L A This feature has been corrected as a result of our quality control procedures. The original label was 'L38A'. Wed May 02 18:20:04 BST 2018 This feature has been corrected as a result of our quality control procedures. The original label was 'leu38ala' Tue Jun 30 17:07:39 BST 2020 This feature has been corrected as a result of our quality control procedures. The original label was 'p.Leu38Ala' in vitro In vitro 9 unspecified role unspecified role unspecified role unspecified role Region 25-138 Region 25-138 sufficient to bind sufficient binding region sufficient to bind certain certain sequence position certain certain certain sequence position certain ecolx Escherichia coli direct interaction direct interaction bud13p-snu17p-2 7 10 unspecified role unspecified role unspecified role unspecified role Region 215-245 Region 215-245 sufficient to bind sufficient binding region sufficient to bind certain certain sequence position certain certain certain sequence position certain ecolx Escherichia coli 9 unspecified role unspecified role unspecified role unspecified role Region 25-138 Region 25-138 sufficient to bind sufficient binding region sufficient to bind certain certain sequence position certain certain certain sequence position certain ecolx Escherichia coli direct interaction direct interaction bud13p-snu17p-3 4 10 unspecified role unspecified role unspecified role unspecified role Region 215-245 Region 215-245 sufficient to bind sufficient binding region sufficient to bind certain certain sequence position certain certain certain sequence position certain P46947:p.Trp232Ala W232A mutation disrupting strength mutation disrupting interaction strength mutation disrupting strength alanine scanning alanine scanning certain certain sequence position certain certain certain sequence position certain W A This feature has been corrected as a result of our quality control procedures. The original label was 'W232A'. Wed May 02 18:36:07 BST 2018 This feature has been corrected as a result of our quality control procedures. The original label was 'trp232ala' Tue Jun 30 18:18:55 BST 2020 This feature has been corrected as a result of our quality control procedures. The original label was 'p.Trp232Ala' P46947:p.Arg237Ala R237A mutation disrupting strength mutation disrupting interaction strength mutation disrupting strength alanine scanning alanine scanning certain certain sequence position certain certain certain sequence position certain R A This feature has been corrected as a result of our quality control procedures. The original label was 'R237A'. Wed May 02 14:58:58 BST 2018 This feature has been corrected as a result of our quality control procedures. The original label was 'arg237ala' Tue Jun 30 18:42:59 BST 2020 This feature has been corrected as a result of our quality control procedures. The original label was 'p.Arg237Ala' P46947:p.Phe224Ala F224A mutation decreasing strength mutation decreasing interaction strength mutation decreasing strength alanine scanning alanine scanning certain certain sequence position certain certain certain sequence position certain F A This feature has been corrected as a result of our quality control procedures. The original label was 'F224A'. Wed May 02 19:16:35 BST 2018 This feature has been corrected as a result of our quality control procedures. The original label was 'phe224ala' Tue Jun 30 15:49:28 BST 2020 This feature has been corrected as a result of our quality control procedures. The original label was 'p.Phe224Ala' P46947:p.Val235Ala V235A mutation decreasing strength mutation decreasing interaction strength mutation decreasing strength alanine scanning alanine scanning certain certain sequence position certain certain certain sequence position certain V A This feature has been corrected as a result of our quality control procedures. The original label was 'V235A'. Wed May 02 18:09:49 BST 2018 This feature has been corrected as a result of our quality control procedures. The original label was 'val235ala' Tue Jun 30 19:54:54 BST 2020 This feature has been corrected as a result of our quality control procedures. The original label was 'p.Val235Ala' in vitro In vitro 9 unspecified role unspecified role unspecified role unspecified role Region 25-138 Region 25-138 sufficient to bind sufficient binding region sufficient to bind certain certain sequence position certain certain certain sequence position certain ecolx Escherichia coli direct interaction direct interaction