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/ Cancer-associated PTEN mutants act in a dominant-negative manner to suppress PTEN protein function. Cancer-associated PTEN mutants act in a dominant-negative manner to suppress PTEN protein function. Cell (0092-8674) 2014 imex curation Papa A., Wan L., Bonora M., Salmena L., Song M.S., Hobbs R.M., Lunardi A., Webster K., Ng C., Newton R.H., Knoblauch N., Guarnerio J., Ito K., Turka L.A., Beck A.H., Pinton P., Bronson R.T., Wei W., Pandolfi P.P. Expts on total lysates (2D, 2F, 2J) not annotated) Interactions involving components of the PI3K complex (p85:p110) were not annotated as these mapped to multiple gene products. ppandolf@bidmc.harvard.edu 15-06-2015: Contacted by IntAct-Help. Only protein-protein interactions in vitro In vitro phosphatase assay phosphatase assay predetermined predetermined participant predetermined Papa A., Wan L., Bonora M., Salmena L., Song M.S., Hobbs R.M., Lunardi A., Webster K., Ng C., Newton R.H., Knoblauch N., Guarnerio J., Ito K., Turka L.A., Beck A.H., Pinton P., Bronson R.T., Wei W., Pandolfi P.P. Expts on total lysates (2D, 2F, 2J) not annotated) Interactions involving components of the PI3K complex (p85:p110) were not annotated as these mapped to multiple gene products. ppandolf@bidmc.harvard.edu Accepted 2015-MAY-15 by PPORRAS Cell (0092-8674) 2014 Only protein-protein interactions imex curation According to Supp Fig. 2A, the GFP is also N-terminal; Fig 2A shows His tag as N-terminal Cancer-associated PTEN mutants act in a dominant-negative manner to suppress PTEN protein function. Cancer-associated PTEN mutants act in a dominant-negative manner to suppress PTEN protein function. Cell (0092-8674) 2014 imex curation Papa A., Wan L., Bonora M., Salmena L., Song M.S., Hobbs R.M., Lunardi A., Webster K., Ng C., Newton R.H., Knoblauch N., Guarnerio J., Ito K., Turka L.A., Beck A.H., Pinton P., Bronson R.T., Wei W., Pandolfi P.P. Expts on total lysates (2D, 2F, 2J) not annotated) Interactions involving components of the PI3K complex (p85:p110) were not annotated as these mapped to multiple gene products. ppandolf@bidmc.harvard.edu 15-06-2015: Contacted by IntAct-Help. Only protein-protein interactions ecoli Escherichia coli (strain K12) pull down pull down anti tag western anti tag western blot anti tag western Papa A., Wan L., Bonora M., Salmena L., Song M.S., Hobbs R.M., Lunardi A., Webster K., Ng C., Newton R.H., Knoblauch N., Guarnerio J., Ito K., Turka L.A., Beck A.H., Pinton P., Bronson R.T., Wei W., Pandolfi P.P. Not sure this is really a pulldown, as they describe anti-GST Abs in the M&Ms but nothing about gluthathione resin but I've gone with what the author said. ppandolf@bidmc.harvard.edu Accepted 2015-MAY-15 by PPORRAS Cell (0092-8674) 2014 imex curation Cancer-associated PTEN mutants act in a dominant-negative manner to suppress PTEN protein function. Cancer-associated PTEN mutants act in a dominant-negative manner to suppress PTEN protein function. Cell (0092-8674) 2014 imex curation Papa A., Wan L., Bonora M., Salmena L., Song M.S., Hobbs R.M., Lunardi A., Webster K., Ng C., Newton R.H., Knoblauch N., Guarnerio J., Ito K., Turka L.A., Beck A.H., Pinton P., Bronson R.T., Wei W., Pandolfi P.P. Expts on total lysates (2D, 2F, 2J) not annotated) Interactions involving components of the PI3K complex (p85:p110) were not annotated as these mapped to multiple gene products. ppandolf@bidmc.harvard.edu 15-06-2015: Contacted by IntAct-Help. Only protein-protein interactions human-pc3 Human PC3 Caucasian prostate adenocarcinoma pc3 Human Caucasian prostate adenocarcinoma comig non denat gel comigration in non denaturing gel electrophoresis comig non denat gel western blot western blot Immuno blot Immuno blot Papa A., Wan L., Bonora M., Salmena L., Song M.S., Hobbs R.M., Lunardi A., Webster K., Ng C., Newton R.H., Knoblauch N., Guarnerio J., Ito K., Turka L.A., Beck A.H., Pinton P., Bronson R.T., Wei W., Pandolfi P.P. Immunoprecipitated lysates were used as an input for the gel run. ppandolf@bidmc.harvard.edu Accepted 2015-MAY-15 by PPORRAS Cell (0092-8674) 2014 imex curation Cancer-associated PTEN mutants act in a dominant-negative manner to suppress PTEN protein function. Cancer-associated PTEN mutants act in a dominant-negative manner to suppress PTEN protein function. Cell (0092-8674) 2014 imex curation Papa A., Wan L., Bonora M., Salmena L., Song M.S., Hobbs R.M., Lunardi A., Webster K., Ng C., Newton R.H., Knoblauch N., Guarnerio J., Ito K., Turka L.A., Beck A.H., Pinton P., Bronson R.T., Wei W., Pandolfi P.P. Expts on total lysates (2D, 2F, 2J) not annotated) Interactions involving components of the PI3K complex (p85:p110) were not annotated as these mapped to multiple gene products. ppandolf@bidmc.harvard.edu 15-06-2015: Contacted by IntAct-Help. Only protein-protein interactions human-pc3 Human PC3 Caucasian prostate adenocarcinoma pc3 Human Caucasian prostate adenocarcinoma bret bioluminescence resonance energy transfer BRET LRET LRET BRET bret tag visualisation tag visualisation Papa A., Wan L., Bonora M., Salmena L., Song M.S., Hobbs R.M., Lunardi A., Webster K., Ng C., Newton R.H., Knoblauch N., Guarnerio J., Ito K., Turka L.A., Beck A.H., Pinton P., Bronson R.T., Wei W., Pandolfi P.P. Administration of Coelenterazine as substrate for the luciferase induced Renilla excitation that generated a BRET signal when in proximity to the GFP ppandolf@bidmc.harvard.edu Accepted 2015-MAY-15 by PPORRAS Cell (0092-8674) 2014 imex curation Cancer-associated PTEN mutants act in a dominant-negative manner to suppress PTEN protein function. Cancer-associated PTEN mutants act in a dominant-negative manner to suppress PTEN protein function. Cell (0092-8674) 2014 imex curation Papa A., Wan L., Bonora M., Salmena L., Song M.S., Hobbs R.M., Lunardi A., Webster K., Ng C., Newton R.H., Knoblauch N., Guarnerio J., Ito K., Turka L.A., Beck A.H., Pinton P., Bronson R.T., Wei W., Pandolfi P.P. Expts on total lysates (2D, 2F, 2J) not annotated) Interactions involving components of the PI3K complex (p85:p110) were not annotated as these mapped to multiple gene products. ppandolf@bidmc.harvard.edu 15-06-2015: Contacted by IntAct-Help. Only protein-protein interactions mouse-nih_3t3 Mus musculus Swiss NIH 3t3 embryo fibroblast cells nih_3t3 Mouse Swiss NIH embryo contact inhibited fibroblast cells comig non denat gel comigration in non denaturing gel electrophoresis comig non denat gel western blot western blot Immuno blot Immuno blot Papa A., Wan L., Bonora M., Salmena L., Song M.S., Hobbs R.M., Lunardi A., Webster K., Ng C., Newton R.H., Knoblauch N., Guarnerio J., Ito K., Turka L.A., Beck A.H., Pinton P., Bronson R.T., Wei W., Pandolfi P.P. PTEN protein was first immunoprecipitated before running on native gel electrophoresis. ppandolf@bidmc.harvard.edu Accepted 2015-MAY-08 by PPORRAS Cell (0092-8674) 2014 imex curation Cancer-associated PTEN mutants act in a dominant-negative manner to suppress PTEN protein function. Cancer-associated PTEN mutants act in a dominant-negative manner to suppress PTEN protein function. Cell (0092-8674) 2014 imex curation Papa A., Wan L., Bonora M., Salmena L., Song M.S., Hobbs R.M., Lunardi A., Webster K., Ng C., Newton R.H., Knoblauch N., Guarnerio J., Ito K., Turka L.A., Beck A.H., Pinton P., Bronson R.T., Wei W., Pandolfi P.P. Expts on total lysates (2D, 2F, 2J) not annotated) Interactions involving components of the PI3K complex (p85:p110) were not annotated as these mapped to multiple gene products. ppandolf@bidmc.harvard.edu 15-06-2015: Contacted by IntAct-Help. Only protein-protein interactions human-pc3 Human PC3 Caucasian prostate adenocarcinoma pc3 Human Caucasian prostate adenocarcinoma anti tag coip anti tag coimmunoprecipitation anti tag coip anti tag western anti tag western blot anti tag western Papa A., Wan L., Bonora M., Salmena L., Song M.S., Hobbs R.M., Lunardi A., Webster K., Ng C., Newton R.H., Knoblauch N., Guarnerio J., Ito K., Turka L.A., Beck A.H., Pinton P., Bronson R.T., Wei W., Pandolfi P.P. ppandolf@bidmc.harvard.edu Accepted 2015-MAY-15 by PPORRAS Cell (0092-8674) 2014 imex curation Cancer-associated PTEN mutants act in a dominant-negative manner to suppress PTEN protein function. Cancer-associated PTEN mutants act in a dominant-negative manner to suppress PTEN protein function. Cell (0092-8674) 2014 imex curation Papa A., Wan L., Bonora M., Salmena L., Song M.S., Hobbs R.M., Lunardi A., Webster K., Ng C., Newton R.H., Knoblauch N., Guarnerio J., Ito K., Turka L.A., Beck A.H., Pinton P., Bronson R.T., Wei W., Pandolfi P.P. Expts on total lysates (2D, 2F, 2J) not annotated) Interactions involving components of the PI3K complex (p85:p110) were not annotated as these mapped to multiple gene products. ppandolf@bidmc.harvard.edu 15-06-2015: Contacted by IntAct-Help. Only protein-protein interactions human-293t Homo sapiens 293 cells transformed with SV40 large T antigen 293t 293 cells expressing SV40 large T antigen. The original designation of this cell line was 293tsA1609neo. It is not in Cabri,ATCC or HyperCLDB. anti tag coip anti tag coimmunoprecipitation anti tag coip western blot western blot Immuno blot Immuno blot Papa A., Wan L., Bonora M., Salmena L., Song M.S., Hobbs R.M., Lunardi A., Webster K., Ng C., Newton R.H., Knoblauch N., Guarnerio J., Ito K., Turka L.A., Beck A.H., Pinton P., Bronson R.T., Wei W., Pandolfi P.P. ppandolf@bidmc.harvard.edu Accepted 2015-MAY-15 by PPORRAS Cell (0092-8674) 2014 imex curation Cancer-associated PTEN mutants act in a dominant-negative manner to suppress PTEN protein function. Cancer-associated PTEN mutants act in a dominant-negative manner to suppress PTEN protein function. Cell (0092-8674) 2014 imex curation Papa A., Wan L., Bonora M., Salmena L., Song M.S., Hobbs R.M., Lunardi A., Webster K., Ng C., Newton R.H., Knoblauch N., Guarnerio J., Ito K., Turka L.A., Beck A.H., Pinton P., Bronson R.T., Wei W., Pandolfi P.P. Expts on total lysates (2D, 2F, 2J) not annotated) Interactions involving components of the PI3K complex (p85:p110) were not annotated as these mapped to multiple gene products. ppandolf@bidmc.harvard.edu 15-06-2015: Contacted by IntAct-Help. Only protein-protein interactions human-pc3 Human PC3 Caucasian prostate adenocarcinoma pc3 Human Caucasian prostate adenocarcinoma comig non denat gel comigration in non denaturing gel electrophoresis comig non denat gel anti tag western anti tag western blot anti tag western Papa A., Wan L., Bonora M., Salmena L., Song M.S., Hobbs R.M., Lunardi A., Webster K., Ng C., Newton R.H., Knoblauch N., Guarnerio J., Ito K., Turka L.A., Beck A.H., Pinton P., Bronson R.T., Wei W., Pandolfi P.P. Immunoprecipitated lysates were used as an input for the gel run. ppandolf@bidmc.harvard.edu Accepted 2015-MAY-15 by PPORRAS Cell (0092-8674) 2014 imex curation pten_mouse Phosphatidylinositol 3,4,5-trisphosphate 3-phosphatase and dual-specificity protein phosphatase PTEN Mutated in multiple advanced cancers 1 Pten Mmac1 Phosphatase and tensin homolog protein protein mouse Mus musculus Mouse MTAIIKEIVSRNKRRYQEDGFDLDLTYIYPNIIAMGFPAERLEGVYRNNIDDVVRFLDSKHKNHYKIYNLCAERHYDTAKFNCRVAQYPFEDHNPPQLELIKPFCEDLDQWLSEDDNHVAAIHCKAGKGRTGVMICAYLLHRGKFLKAQEALDFYGEVRTRDKKGVTIPSQRRYVYYYSYLLKNHLDYRPVALLFHKMMFETIPMFSGGTCNPQFVVCQLKVKIYSSNSGPTRREDKFMYFEFPQPLPVCGDIKVEFFHKQNKMLKKDKMFHFWVNTFFIPGPEETSEKVENGSLCDQEIDSICSIERADNDKEYLVLTLTKNDLDKANKDKANRYFSPNFKVKLYFTKTVEEPSNPEASSSTSVTPDVSDNEPDHYRYSDTTDSDPENEPFDEDQHSQITKV DIP protein O08586 original sequence version: 125 DIP protein O08586 original sequence version: 81 DIP protein O08586 original sequence version: 129 DIP protein O08586 original sequence version: 154 75F97C3DD6843BA9 1-phosphatidyl-1d-myo-inositol 3,4,5-trisphosphate 1-phosphatidyl-1D-myo-inositol 3,4,5-trisphosphates small molecule small molecule chemical synthesis Chemical synthesis (Chemical synthesis) pten_human Phosphatidylinositol 3,4,5-trisphosphate 3-phosphatase and dual-specificity protein phosphatase PTEN Phosphatase and tensin homolog Mutated in multiple advanced cancers 1 PTEN MMAC1 TEP1 protein protein human Homo sapiens Human MTAIIKEIVSRNKRRYQEDGFDLDLTYIYPNIIAMGFPAERLEGVYRNNIDDVVRFLDSKHKNHYKIYNLCAERHYDTAKFNCRVAQYPFEDHNPPQLELIKPFCEDLDQWLSEDDNHVAAIHCKAGKGRTGVMICAYLLHRGKFLKAQEALDFYGEVRTRDKKGVTIPSQRRYVYYYSYLLKNHLDYRPVALLFHKMMFETIPMFSGGTCNPQFVVCQLKVKIYSSNSGPTRREDKFMYFEFPQPLPVCGDIKVEFFHKQNKMLKKDKMFHFWVNTFFIPGPEETSEKVENGSLCDQEIDSICSIERADNDKEYLVLTLTKNDLDKANKDKANRYFSPNFKVKLYFTKTVEEPSNPEASSSTSVTPDVSDNEPDHYRYSDTTDSDPENEPFDEDQHTQITKV 75F97C3DD6802BA9 pten-pten-1 6 11 unspecified role unspecified role bait bait n-terminal myc tag myc tag EUKLISEED epitope tag EUKLISEED epitope tag n-term range n-terminal range n-term range n-term range n-terminal range n-term range 11 unspecified role unspecified role prey prey n-terminal gfp tag green fluorescent protein tag GFP green fluorescent protein GFP green fluorescent protein gfp tag n-term range n-terminal range n-term range n-term range n-terminal range n-term range physical association physical association Fig. 1A, 3B, 6D, 7C, Supp. Fig. 1B, 1C, 2B PTEN uses multiple interfaces along the entire protein to dimerize pten-pten-2 6 11 unspecified role unspecified role prey prey n-terminal myc tag myc tag EUKLISEED epitope tag EUKLISEED epitope tag n-term range n-terminal range n-term range n-term range n-terminal range n-term range 11 unspecified role unspecified role bait bait n-terminal gfp tag green fluorescent protein tag GFP green fluorescent protein GFP green fluorescent protein gfp tag n-term range n-terminal range n-term range n-term range n-terminal range n-term range physical association physical association Fig. 1A pten-pten-3 7 11 unspecified role unspecified role bait bait n-terminal gfp tag green fluorescent protein tag GFP green fluorescent protein GFP green fluorescent protein gfp tag n-term range n-terminal range n-term range n-term range n-terminal range n-term range 11 unspecified role unspecified role prey prey physical association physical association Fig. 1B pten-8 5 9 unspecified role unspecified role neutral component neutral component physical association physical association 1C pten-pten-4 2 11 unspecified role unspecified role bait bait n-terminal 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 11 unspecified role unspecified role prey prey n-terminal his tag his tag Hexa-His-tag 6-His-tag Histidine-tag Hexa-His-tag Histidine-tag 6-His-tag n-term range n-terminal range n-term range n-term range n-terminal range n-term range physical association physical association Fig. 1D, 2B, 3D, 7B PTEN uses multiple interfaces along the entire protein to dimerise. pten-pten-6 4 11 proton donor proton donor neutral component neutral component region renilla luciferase renilla luciferase protein tag renilla luciferase undetermined undetermined sequence position undetermined undetermined undetermined sequence position undetermined 11 proton acceptor proton acceptor neutral component neutral component region gfp tag green fluorescent protein tag GFP green fluorescent protein GFP green fluorescent protein gfp tag n-term range n-terminal range n-term range n-term range n-terminal range n-term range proximity proximity close-contact colocalization neighbourhood interaction Fig. 1E, 1F, 1H, 3C pten-pten-7 4 11 proton donor proton donor neutral component neutral component region renilla luciferase renilla luciferase protein tag renilla luciferase undetermined undetermined sequence position undetermined undetermined undetermined sequence position undetermined 11 competitor competitor competitor neutral component neutral component 11 proton acceptor proton acceptor neutral component neutral component region gfp tag green fluorescent protein tag GFP green fluorescent protein GFP green fluorescent protein gfp tag n-term range n-terminal range n-term range n-term range n-terminal range n-term range proximity proximity close-contact colocalization neighbourhood interaction Fig. 1G pten-1 8 11 unspecified role unspecified role neutral component neutral component n-terminal myc tag myc tag EUKLISEED epitope tag EUKLISEED epitope tag n-term range n-terminal range n-term range n-term range n-terminal range n-term range physical association physical association Fig. 2I, 3A Supp. Fig. 1D, 2H Point mutation and western blot data suggests phosphorylation of the C-terminal tail maintains PTEN as a monomer pten-pten-12 3 11 unspecified role unspecified role neutral component neutral component n-terminal myc tag myc tag EUKLISEED epitope tag EUKLISEED epitope tag n-term range n-terminal range n-term range n-term range n-terminal range n-term range physical association physical association Supp. Fig. 1A pten-pten-11 6 11 unspecified role unspecified role bait bait n-terminal 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 region sufficient to bind sufficient binding region sufficient to bind certain certain sequence position certain certain certain sequence position certain 11 unspecified role unspecified role prey prey n-terminal myc tag myc tag EUKLISEED epitope tag EUKLISEED epitope tag n-term range n-terminal range n-term range n-term range n-terminal range n-term range physical association physical association Supp. Fig. 2D PTEN uses multiple interfaces along the entire protein to dimerize 1_phosphatidyl_1d_myo_inositol_3_4_5_trisphosphate-pten-1 1 10 enzyme target enzyme target substrate substrate neutral component neutral component 11 enzyme enzyme neutral component neutral component n-terminal 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 P60484:p.Cys124Ser mutation decreasing rate mutation decreasing interaction rate mutation decreasing rate certain certain sequence position certain certain certain sequence position certain C S Wed May 02 17:02:05 BST 2018 This feature has been corrected as a result of our quality control procedures. The original label was 'cys124ser' Tue Jun 30 19:20:32 BST 2020 This feature has been corrected as a result of our quality control procedures. The original label was 'p.Cys124Ser' P60484:p.Gly129Glu mutation decreasing rate mutation decreasing interaction rate mutation decreasing rate certain certain sequence position certain certain certain sequence position certain G E Wed May 02 17:03:34 BST 2018 This feature has been corrected as a result of our quality control procedures. The original label was 'gly129glu' Tue Jun 30 17:59:26 BST 2020 This feature has been corrected as a result of our quality control procedures. The original label was 'p.Gly129Glu' P60484:p.Arg130Gly mutation decreasing rate mutation decreasing interaction rate mutation decreasing rate certain certain sequence position certain certain certain sequence position certain R G Wed May 02 19:33:49 BST 2018 This feature has been corrected as a result of our quality control procedures. The original label was 'arg130gly' Tue Jun 30 19:34:30 BST 2020 This feature has been corrected as a result of our quality control procedures. The original label was 'p.Arg130Gly' ecoli Escherichia coli (strain K12) 11 enzyme enzyme unspecified role unspecified role n-terminal his tag his tag Hexa-His-tag 6-His-tag Histidine-tag Hexa-His-tag Histidine-tag 6-His-tag n-term range n-terminal range n-term range n-term range n-terminal range n-term range ecoli Escherichia coli (strain K12) dephosphorylation dephosphorylation reaction dephosphorylation Fig. 3E, 7D