UniProt UniProt http://www.uniprot.org FUS interacts with nuclear matrix-associated protein SAFB1 as well as Matrin3 to regulate splicing and ligand-mediated transcription. FUS interacts with nuclear matrix-associated protein SAFB1 as well as Matrin3 to regulate splicing and ligand-mediated transcription. Scientific reports 2016 imex curation Yamaguchi A., Takanashi K. atsyama@restaff.chiba-u.jp 25-Jul-2019: Contacted by IntAct-Help. Only protein-protein interactions imex curation human-293 Homo sapiens transformed primary embryonal kidney cells Human 293 Transformed human primary embryonal kidney cells. The Cell type named 293 is synonymous with HEK-293. anti tag coip anti tag coimmunoprecipitation anti tag coip western blot western blot Immuno blot Immuno blot Yamaguchi A., Takanashi K. atsyama@restaff.chiba-u.jp Accepted 2019-MAY-24 AT 09:32 BST AT 09:32 BST by MGT Scientific reports 2016 Only protein-protein interactions imex curation imex curation "Arrows indicate the co-localizations." - there are no arrows on the top row, the unmutated protein is in a different subcellular location, and the comment is there on both interactions. I did miss the Addgene reference. Interactions now added - no idea where the data-processing comment went. FUS interacts with nuclear matrix-associated protein SAFB1 as well as Matrin3 to regulate splicing and ligand-mediated transcription. FUS interacts with nuclear matrix-associated protein SAFB1 as well as Matrin3 to regulate splicing and ligand-mediated transcription. Scientific reports 2016 imex curation Yamaguchi A., Takanashi K. atsyama@restaff.chiba-u.jp 25-Jul-2019: Contacted by IntAct-Help. Only protein-protein interactions imex curation yeasx Saccharomyces cerevisiae (Baker's yeast) Baker's yeast 2 hybrid two hybrid 2H 2h Gal4 transcription regeneration two-hybrid yeast two hybrid 2-hybrid classical two hybrid classical two hybrid 2H two-hybrid 2-hybrid Gal4 transcription regeneration 2h yeast two hybrid Y2H Y-2H 2 hybrid nucleotide sequence nucleotide sequence identification sequence cloning sequence cloning nucleotide sequence Yamaguchi A., Takanashi K. atsyama@restaff.chiba-u.jp Accepted 2019-MAY-24 AT 09:32 BST AT 09:32 BST by MGT Human brain cDNA Scientific reports 2016 Only protein-protein interactions imex curation imex curation "Arrows indicate the co-localizations." - there are no arrows on the top row, the unmutated protein is in a different subcellular location, and the comment is there on both interactions. I did miss the Addgene reference. Interactions now added - no idea where the data-processing comment went. FUS interacts with nuclear matrix-associated protein SAFB1 as well as Matrin3 to regulate splicing and ligand-mediated transcription. FUS interacts with nuclear matrix-associated protein SAFB1 as well as Matrin3 to regulate splicing and ligand-mediated transcription. Scientific reports 2016 imex curation Yamaguchi A., Takanashi K. atsyama@restaff.chiba-u.jp 25-Jul-2019: Contacted by IntAct-Help. Only protein-protein interactions imex curation human-293 Homo sapiens transformed primary embryonal kidney cells Human 293 Transformed human primary embryonal kidney cells. The Cell type named 293 is synonymous with HEK-293. anti bait coip anti bait coimmunoprecipitation anti bait coip western blot western blot Immuno blot Immuno blot Yamaguchi A., Takanashi K. atsyama@restaff.chiba-u.jp Accepted 2019-MAY-24 AT 09:32 BST AT 09:32 BST by MGT Scientific reports 2016 Only protein-protein interactions imex curation imex curation "Arrows indicate the co-localizations." - there are no arrows on the top row, the unmutated protein is in a different subcellular location, and the comment is there on both interactions. I did miss the Addgene reference. Interactions now added - no idea where the data-processing comment went. FUS interacts with nuclear matrix-associated protein SAFB1 as well as Matrin3 to regulate splicing and ligand-mediated transcription. FUS interacts with nuclear matrix-associated protein SAFB1 as well as Matrin3 to regulate splicing and ligand-mediated transcription. Scientific reports 2016 imex curation Yamaguchi A., Takanashi K. atsyama@restaff.chiba-u.jp 25-Jul-2019: Contacted by IntAct-Help. Only protein-protein interactions imex curation human-293 Homo sapiens transformed primary embryonal kidney cells Human 293 Transformed human primary embryonal kidney cells. The Cell type named 293 is synonymous with HEK-293. fluorescence imaging fluorescence microscopy fluorescence imaging immunocytochemistry immunocytochemistry Yamaguchi A., Takanashi K. atsyama@restaff.chiba-u.jp Accepted 2019-MAY-24 AT 09:32 BST AT 09:32 BST by MGT Scientific reports 2016 Only protein-protein interactions imex curation imex curation "Arrows indicate the co-localizations." - there are no arrows on the top row, the unmutated protein is in a different subcellular location, and the comment is there on both interactions. I did miss the Addgene reference. Interactions now added - no idea where the data-processing comment went. FUS interacts with nuclear matrix-associated protein SAFB1 as well as Matrin3 to regulate splicing and ligand-mediated transcription. FUS interacts with nuclear matrix-associated protein SAFB1 as well as Matrin3 to regulate splicing and ligand-mediated transcription. Scientific reports 2016 imex curation Yamaguchi A., Takanashi K. atsyama@restaff.chiba-u.jp 25-Jul-2019: Contacted by IntAct-Help. Only protein-protein interactions imex curation human-sh_sy5y Homo sapiens SH-SY5Y cell line sh_sy5y Human neuroblastoma cells confocal microscopy confocal microscopy immunocytochemistry immunocytochemistry Yamaguchi A., Takanashi K. atsyama@restaff.chiba-u.jp Accepted 2019-MAY-24 AT 09:32 BST AT 09:32 BST by MGT Scientific reports 2016 Only protein-protein interactions imex curation imex curation "Arrows indicate the co-localizations." - there are no arrows on the top row, the unmutated protein is in a different subcellular location, and the comment is there on both interactions. I did miss the Addgene reference. Interactions now added - no idea where the data-processing comment went. FUS interacts with nuclear matrix-associated protein SAFB1 as well as Matrin3 to regulate splicing and ligand-mediated transcription. FUS interacts with nuclear matrix-associated protein SAFB1 as well as Matrin3 to regulate splicing and ligand-mediated transcription. Scientific reports 2016 imex curation Yamaguchi A., Takanashi K. atsyama@restaff.chiba-u.jp 25-Jul-2019: Contacted by IntAct-Help. Only protein-protein interactions imex curation human-sh_sy5y Homo sapiens SH-SY5Y cell line sh_sy5y Human neuroblastoma cells fluorescence imaging fluorescence microscopy fluorescence imaging immunocytochemistry immunocytochemistry Yamaguchi A., Takanashi K. atsyama@restaff.chiba-u.jp Accepted 2019-MAY-24 AT 09:32 BST AT 09:32 BST by MGT Scientific reports 2016 Only protein-protein interactions imex curation imex curation "Arrows indicate the co-localizations." - there are no arrows on the top row, the unmutated protein is in a different subcellular location, and the comment is there on both interactions. I did miss the Addgene reference. Interactions now added - no idea where the data-processing comment went. FUS interacts with nuclear matrix-associated protein SAFB1 as well as Matrin3 to regulate splicing and ligand-mediated transcription. FUS interacts with nuclear matrix-associated protein SAFB1 as well as Matrin3 to regulate splicing and ligand-mediated transcription. Scientific reports 2016 imex curation Yamaguchi A., Takanashi K. atsyama@restaff.chiba-u.jp 25-Jul-2019: Contacted by IntAct-Help. Only protein-protein interactions imex curation in vitro In vitro pull down pull down western blot western blot Immuno blot Immuno blot Yamaguchi A., Takanashi K. atsyama@restaff.chiba-u.jp Accepted 2019-MAY-24 AT 09:32 BST AT 09:32 BST by MGT Scientific reports 2016 Only protein-protein interactions imex curation imex curation "Arrows indicate the co-localizations." - there are no arrows on the top row, the unmutated protein is in a different subcellular location, and the comment is there on both interactions. I did miss the Addgene reference. Interactions now added - no idea where the data-processing comment went. FUS interacts with nuclear matrix-associated protein SAFB1 as well as Matrin3 to regulate splicing and ligand-mediated transcription. FUS interacts with nuclear matrix-associated protein SAFB1 as well as Matrin3 to regulate splicing and ligand-mediated transcription. Scientific reports 2016 imex curation Yamaguchi A., Takanashi K. atsyama@restaff.chiba-u.jp 25-Jul-2019: Contacted by IntAct-Help. Only protein-protein interactions imex curation mouse-spinal-cord Mouse spinal cord spinal-cord spinal cord fluorescence imaging fluorescence microscopy fluorescence imaging immunohistochemistry immunohistochemistry Yamaguchi A., Takanashi K. atsyama@restaff.chiba-u.jp Accepted 2019-MAY-24 AT 09:32 BST AT 09:32 BST by MGT Scientific reports 2016 Only protein-protein interactions imex curation imex curation "Arrows indicate the co-localizations." - there are no arrows on the top row, the unmutated protein is in a different subcellular location, and the comment is there on both interactions. I did miss the Addgene reference. Interactions now added - no idea where the data-processing comment went. safb1_human Scaffold attachment factor B1 SAFB HAP HET SAFB1 HSP27 estrogen response element-TATA box-binding protein protein protein human Homo sapiens Human MAETLSGLGDSGAAGAAALSSASSETGTRRLSDLRVIDLRAELRKRNVDSSGNKSVLMERLKKAIEDEGGNPDEIEITSEGNKKTSKRSSKGRKPEEEGVEDNGLEENSGDGQEDVETSLENLQDIDIMDISVLDEAEIDNGSVADCVEDDDADNLQESLSDSRELVEGEMKELPEQLQEHAIEDKETINNLDTSSSDFTILQEIEEPSLEPENEKILDILGETCKSEPVKEESSELEQPFAQDTSSVGPDRKLAEEEDLFDSAHPEEGDLDLASESTAHAQSSKADSLLAVVKREPAEQPGDGERTDCEPVGLEPAVEQSSAASELAEASSEELAEAPTEAPSPEARDSKEDGRKFDFDACNEVPPAPKESSTSEGADQKMSSPEDDSDTKRLSKEEKGRSSCGRNFWVSGLSSTTRATDLKNLFSKYGKVVGAKVVTNARSPGARCYGFVTMSTAEEATKCINHLHKTELHGKMISVEKAKNEPVGKKTSDKRDSDGKKEKSSNSDRSTNLKRDDKCDRKDDAKKGDDGSGEKSKDQDDQKPGPSERSRATKSGSRGTERTVVMDKSKGVPVISVKTSGSKERASKSQDRKSASREKRSVVSFDKVKEPRKSRDSESHSRVRERSEREQRMQAQWEREERERLEIARERLAFQRQRLERERMERERLERERMHVEHERRREQERIHREREELRRQQELRYEQERRPAVRRPYDLDRRDDAYWPEAKRAALDERYHSDFNRQDRFHDFDHRDRGRYPDHSVDRREGSRSMMGEREGQHYPERHGGPERHGRDSRDGWGGYGSDKRMSEGRGLPPPPRRDWGDHGRREDDRSWQGTADGGMMDRDHKRWQGGERSMSGHSGPGHMMNRGGMSGRGSFAPGGASRGHPIPHGGMQGGFGGQSRGSRPSDARFTRRY E865940BC7783C4A andr_human Androgen receptor Dihydrotestosterone receptor Nuclear receptor subfamily 3 group C member 4 AR DHTR NR3C4 protein protein human Homo sapiens Human MEVQLGLGRVYPRPPSKTYRGAFQNLFQSVREVIQNPGPRHPEAASAAPPGASLLLLQQQQQQQQQQQQQQQQQQQQQQQETSPRQQQQQQGEDGSPQAHRRGPTGYLVLDEEQQPSQPQSALECHPERGCVPEPGAAVAASKGLPQQLPAPPDEDDSAAPSTLSLLGPTFPGLSSCSADLKDILSEASTMQLLQQQQQEAVSEGSSSGRAREASGAPTSSKDNYLGGTSTISDNAKELCKAVSVSMGLGVEALEHLSPGEQLRGDCMYAPLLGVPPAVRPTPCAPLAECKGSLLDDSAGKSTEDTAEYSPFKGGYTKGLEGESLGCSGSAAAGSSGTLELPSTLSLYKSGALDEAAAYQSRDYYNFPLALAGPPPPPPPPHPHARIKLENPLDYGSAWAAAAAQCRYGDLASLHGAGAAGPGSGSPSAAASSSWHTLFTAEEGQLYGPCGGGGGGGGGGGGGGGGGGGGGGGEAGAVAPYGYTRPPQGLAGQESDFTAPDVWYPGGMVSRVPYPSPTCVKSEMGPWMDSYSGPYGDMRLETARDHVLPIDYYFPPQKTCLICGDEASGCHYGALTCGSCKVFFKRAAEGKQKYLCASRNDCTIDKFRRKNCPSCRLRKCYEAGMTLGARKLKKLGNLKLQEEGEASSTTSPTEETTQKLTVSHIEGYECQPIFLNVLEAIEPGVVCAGHDNNQPDSFAALLSSLNELGERQLVHVVKWAKALPGFRNLHVDDQMAVIQYSWMGLMVFAMGWRSFTNVNSRMLYFAPDLVFNEYRMHKSRMYSQCVRMRHLSQEFGWLQITPQEFLCMKALLLFSIIPVDGLKNQKFFDELRMNYIKELDRIIACKRKNPTSCSRRFYQLTKLLDSVQPIARELHQFTFDLLIKSHMVSVDFPEMMAEIISVQVPKILSGKVKPIYFHTQ DIP protein P10275 original sequence version: 220 DIP protein P10275-1 original sequence version: 213 DIP protein P10275 original sequence version: 216 DIP protein P10275 original sequence version: 143 DIP protein P10275 original sequence version: 174 DIP protein P10275 original sequence version: 169 DIP protein P10275 original sequence version: 188 DIP protein P10275-1 original sequence version: 188 DIP protein P10275 original sequence version: 196 DIP protein P10275 original sequence version: 217 DIP protein P10275-1 original sequence version: 217 DIP protein P10275-1 original sequence version: 207 A73432C55D39AE06 fus_human RNA-binding protein FUS FUS TLS Oncogene FUS Oncogene TLS Translocated in liposarcoma protein POMp75 75 kDa DNA-pairing protein protein protein human Homo sapiens Human MASNDYTQQATQSYGAYPTQPGQGYSQQSSQPYGQQSYSGYSQSTDTSGYGQSSYSSYGQSQNTGYGTQSTPQGYGSTGGYGSSQSSQSSYGQQSSYPGYGQQPAPSSTSGSYGSSSQSSSYGQPQSGSYSQQPSYGGQQQSYGQQQSYNPPQGYGQQNQYNSSSGGGGGGGGGGNYGQDQSSMSSGGGSGGGYGNQDQSGGGGSGGYGQQDRGGRGRGGSGGGGGGGGGGYNRSSGGYEPRGRGGGRGGRGGMGGSDRGGFNKFGGPRDQGSRHDSEQDNSDNNTIFVQGLGENVTIESVADYFKQIGIIKTNKKTGQPMINLYTDRETGKLKGEATVSFDDPPSAKAAIDWFDGKEFSGNPIKVSFATRRADFNRGGGNGRGGRGRGGPMGRGGYGGGGSGGGGRGGFPSGGGGGGGQQRAGDWKCPNPTCENMNFSWRNECNQCKAPKPDGPGGGPGGSHMGGNYGDDRRGGRGGYDRGGYRGRGGDRGGFRGGRGGGDRGGFGPGKMDSRGEHRQDRRERPY DIP protein P35637 original sequence version: 165 DIP protein P35637 original sequence version: 156 DIP protein P35637-1 original sequence version: 156 DIP protein P35637-1 original sequence version: 92 DIP protein P35637-1 original sequence version: 146 88C8E263B7905549 safb1_mouse Scaffold attachment factor B1 Safb Safb1 protein protein mouse Mus musculus Mouse MAETLSGLGDASAAGAAAVSSAASETGTRRLSDLRVIDLRAELKKRNLDSSGNKSVLMERLKKAIEDEGGNPDEIEVTSECNKKMPKRPSKGRKPEDEGVEDNGLEENSGDGQEDVETSLENLQDMDMMDISVLDEADIDNGSVADCVEEEEEATLPEGLADSTELVEGDLKGLPEQLQEHAIDDKDTVNNVDTSSSDFTMLQEMEEASLEPENEKILDILGETCKSEPVKEEGSELEQPFAQATSSVGPDRKLAEEEDLFESCGHPEEEEEEEEEDQEEEQEEEGDLALASSSKSESPSTRCQWSEADAPLAVVKREPADAPGGGTGMDREPVGLEEPVEQSSTAAQLPEATSQELVRAPTAALSPEPQDSKEDVKKFAFDACNDVPAPPKESSASEGADQKMSSVEEDSDTKRLSREEKGRSSCGRNFWVSGLSSTTRATDLKNLFSRYGKVVGAKVVTNARSPGARCYGFVTMSTAEEATKCISHLHKTELHGKMISVEKAKSEPTGKRVPDRRDGDSKKEKASTSDRSANLKREEKGERKDDAKKTDDGSTEKSKDADDQKPGPSERSRTTKSGSRGTERTVVMDKSKGVPVISVKTSGSKERASKSQDRKSASREKRSVVSFDKVKESRKSRDSESRRERERSEREQRLQAQWEREERERLEIARERLAFHRHRLERERMERERLERERMHVEQERRREQERIHREREELRRQQELRYEQERRPAVRRPYEVDGRRDDAYWPEAKRAALDDRYHSDFSRQDRFHDFDHRDRGRYPNHSVDRREGSRSMMGDREGQHYPERHGGPERHGRDSRDGWGYGSNKRLSEGRGLPPPPRRDWGEHGRRLEDDRAWQGTADGGMMERDHKRWQGGERSMSGHSGPGHMMNRGGMSGRGSFAPGGASRGHVIPRGGMQAGFGGQSRGSRPSDARFTRRY Author screened murine library then identified protein by homology to rat. Currently no murine sequence in database. D246A419FA465C3D matr3_human Matrin-3 KIAA0723 MATR3 protein protein human Homo sapiens Human MSKSFQQSSLSRDSQGHGRDLSAAGIGLLAAATQSLSMPASLGRMNQGTARLASLMNLGMSSSLNQQGAHSALSSASTSSHNLQSIFNIGSRGPLPLSSQHRGDADQASNILASFGLSARDLDELSRYPEDKITPENLPQILLQLKRRRTEEGPTLSYGRDGRSATREPPYRVPRDDWEEKRHFRRDSFDDRGPSLNPVLDYDHGSRSQESGYYDRMDYEDDRLRDGERCRDDSFFGETSHNYHKFDSEYERMGRGPGPLQERSLFEKKRGAPPSSNIEDFHGLLPKGYPHLCSICDLPVHSNKEWSQHINGASHSRRCQLLLEIYPEWNPDNDTGHTMGDPFMLQQSTNPAPGILGPPPPSFHLGGPAVGPRGNLGAGNGNLQGPRHMQKGRVETSRVVHIMDFQRGKNLRYQLLQLVEPFGVISNHLILNKINEAFIEMATTEDAQAAVDYYTTTPALVFGKPVRVHLSQKYKRIKKPEGKPDQKFDQKQELGRVIHLSNLPHSGYSDSAVLKLAEPYGKIKNYILMRMKSQAFIEMETREDAMAMVDHCLKKALWFQGRCVKVDLSEKYKKLVLRIPNRGIDLLKKDKSRKRSYSPDGKESPSDKKSKTDGSQKTESSTEGKEQEEKSGEDGEKDTKDDQTEQEPNMLLESEDELLVDEEEAAALLESGSSVGDETDLANLGDVASDGKKEPSDKAVKKDGSASAAAKKKLKKVDKIEELDQENEAALENGIKNEENTEPGAESSENADDPNKDTSENADGQSDENKDDYTIPDEYRIGPYQPNVPVGIDYVIPKTGFYCKLCSLFYTNEEVAKNTHCSSLPHYQKLKKFLNKLAEERRQKKET 530AA49214BC1611 fus_mouse RNA-binding protein FUS Fus Protein pigpen protein protein mouse Mus musculus Mouse MASNDYTQQATQSYGAYPTQPGQGYSQQSSQPYGQQSYSGYGQSADTSGYGQSSYGSSYGQTQNTGYGTQSAPQGYGSTGGYGSSQSSQSSYGQQSSYPGYGQQPAPSSTSGSYGGSSQSSSYGQPQSGGYGQQSGYGGQQQSYGQQQSSYNPPQGYGQQNQYNSSSGGGGGGGGGNYGQDQSSMSGGGGGGGYGNQDQSGGGGGGYGGGQQDRGGRGRGGGGGYNRSSGGYEPRGRGGGRGGRGGMGGSDRGGFNKFGGPRDQGSRHDSEQDNSDNNTIFVQGLGENVTIESVADYFKQIGIIKTNKKTGQPMINLYTDRETGKLKGEATVSFDDPPSAKAAIDWFDGKEFSGNPIKVSFATRRADFNRGGGNGRGGRGRGGPMGRGGYGGGGSGGGGRGGFPSGGGGGGGQQRAGDWKCPNPTCENMNFSWRNECNQCKAPKPDGPGGGPGGSHMGGNYGDDRRGRGGYDRGGYRGRGGDRGGFRGGRGGGDRGGFGPGKMDSRGEHRQDRRERPY E06F231BFEED78D6 fus-safb-1 2 9 unspecified role unspecified role prey prey over-expressed over expressed level over-expressed 11 unspecified role unspecified role bait bait over-expressed over expressed level over-expressed physical association physical association fus-safb-2 3 9 unspecified role unspecified role prey prey physiological level physiological level endogenous level endogenous endogenous endogenous level 11 unspecified role unspecified role bait bait physiological level physiological level endogenous level endogenous endogenous endogenous level physical association physical association Fig. 1A, Supp. Fig 2A Cell lysates were immunoprecipitated with anti-FUS antibody, and subjected to Western blot with anti-SAFB1 antibody (Fig. 1A). Chromatic was sonication-sheared. Interaction still observed when cells were treated with RNase fus-safb-3 5 9 unspecified role unspecified role neutral component neutral component physiological level physiological level endogenous level endogenous endogenous endogenous level fixed cell fixed cell 11 unspecified role unspecified role neutral component neutral component physiological level physiological level endogenous level endogenous endogenous endogenous level fixed cell fixed cell colocalization colocalization Fig. 1B, 2E Cells were treated with RNase, DNase I or micrococcal nuclease to demonstrate lack of dependence of interaction on nucleic acid binding. Cells were treated with non-ionic detergents, high-salt buffer, and nuclease (‘+TritonX 0.5%, +Salt, + DNase') to produce nuclear matrices. fus-safb-4 7 9 unspecified role unspecified role prey prey over-expressed over expressed level over-expressed cell lysate cell lysate region myc tag myc tag EUKLISEED epitope tag EUKLISEED epitope tag undetermined undetermined sequence position undetermined undetermined undetermined sequence position undetermined human-293 Homo sapiens transformed primary embryonal kidney cells Human 293 Transformed human primary embryonal kidney cells. The Cell type named 293 is synonymous with HEK-293. 11 weight by comassie molecular weight estimation by coomasie staining weight by comassie western blot western blot Immuno blot Immuno blot unspecified role unspecified role bait bait purified purified n-terminus 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 ecoli Escherichia coli (strain K12) physical association physical association Fig. 1D, Supp Fig 2D Chromatic was sonication-sheared. Pulldowns were treated with RNase, DNase I or micrococcal nuclease; no SAFB1 band was seen in the presence of DNase I. Full-length FUS appears to be required for the binding in this assay fus-safb-5 8 12 unspecified role unspecified role neutral component neutral component physiological level physiological level endogenous level endogenous endogenous endogenous level fixed cell fixed cell 14 unspecified role unspecified role neutral component neutral component physiological level physiological level endogenous level endogenous endogenous endogenous level fixed cell fixed cell colocalization colocalization Fig. 2A, 2B Cells were treated with RNase, DNase I or micrococcal nuclease fus-matr3-1 3 13 unspecified role unspecified role prey prey physiological level physiological level endogenous level endogenous endogenous endogenous level 9 unspecified role unspecified role prey prey physiological level physiological level endogenous level endogenous endogenous endogenous level 11 unspecified role unspecified role bait bait physiological level physiological level endogenous level endogenous endogenous endogenous level association association Fig. 5A Chromatic was sonication-sheared fus-matr3-2 5 13 unspecified role unspecified role neutral component neutral component physiological level physiological level endogenous level endogenous endogenous endogenous level fixed cell fixed cell 11 unspecified role unspecified role neutral component neutral component physiological level physiological level endogenous level endogenous endogenous endogenous level fixed cell fixed cell colocalization colocalization Fig. 5B Cells were treated with RNase, DNase I or micrococcal nuclease to demonstrate lack of dependence of interaction on nucleic acid binding. Cells were treated with non-ionic detergents, high-salt buffer, and nuclease (‘+TritonX 0.5%, +Salt, + DNase') to produce nuclear matrices. fus-safb-6 4 9 unspecified role unspecified role neutral component neutral component physiological level physiological level endogenous level endogenous endogenous endogenous level fixed cell fixed cell 11 unspecified role unspecified role neutral component neutral component physiological level physiological level endogenous level endogenous endogenous endogenous level fixed cell fixed cell P35637:p.Pro525Leu mutation mutation certain certain sequence position certain certain certain sequence position certain P L Tue Jun 30 16:51:38 BST 2020 This feature has been corrected as a result of our quality control procedures. The original label was 'p.Pro525Leu' region ha tag ha tag YPYDVPDYA epitope tag YPYDVPDYA epitope tag undetermined undetermined sequence position undetermined undetermined undetermined sequence position undetermined colocalization colocalization Fig. 5D FUS Pro525Leu localises in the cytoplasm and binds to SAFB fus-matr3-3 4 13 unspecified role unspecified role neutral component neutral component physiological level physiological level endogenous level endogenous endogenous endogenous level fixed cell fixed cell 11 unspecified role unspecified role neutral component neutral component physiological level physiological level endogenous level endogenous endogenous endogenous level fixed cell fixed cell P35637:p.Pro525Leu mutation mutation certain certain sequence position certain certain certain sequence position certain P L Tue Jun 30 15:59:45 BST 2020 This feature has been corrected as a result of our quality control procedures. The original label was 'p.Pro525Leu' region ha tag ha tag YPYDVPDYA epitope tag YPYDVPDYA epitope tag undetermined undetermined sequence position undetermined undetermined undetermined sequence position undetermined colocalization colocalization Fig. 5D FUS Pro525Leu localises in the cytoplasm and binds to Matrin-3 fus-safb-7 6 9 unspecified role unspecified role neutral component neutral component physiological level physiological level endogenous level endogenous endogenous endogenous level fixed cell fixed cell 11 unspecified role unspecified role neutral component neutral component physiological level physiological level endogenous level endogenous endogenous endogenous level fixed cell fixed cell colocalization colocalization Fig. 2C Cells were treated with RNase, DNase I or micrococcal nuclease to demonstrate lack of dependence of interaction on nucleic acid binding. Cells were treated with non-ionic detergents, high-salt buffer, and nuclease (‘+TritonX 0.5%, +Salt, + DNase') to produce nuclear matrices. ar-fus-1 1 11 unspecified role unspecified role prey prey physiological level physiological level endogenous level endogenous endogenous endogenous level 9 unspecified role unspecified role prey prey physiological level physiological level endogenous level endogenous endogenous endogenous level 10 unspecified role unspecified role bait bait over-expressed over expressed level over-expressed n-terminal egfp tag enhanced green fluorescent protein tag enhanced green fluorescent protein EGFP enhanced green fluorescent protein EGFP egfp tag n-term range n-terminal range n-term range n-term range n-terminal range n-term range association association Fig. 4C ar-fus-2 4 11 unspecified role unspecified role neutral component neutral component physiological level physiological level endogenous level endogenous endogenous endogenous level 10 tag fluorescence tag visualisation by fluorescence tag fluorescence immunocytochemistry immunocytochemistry unspecified role unspecified role neutral component neutral component over-expressed over expressed level over-expressed n-terminal egfp tag enhanced green fluorescent protein tag enhanced green fluorescent protein EGFP enhanced green fluorescent protein EGFP egfp tag n-term range n-terminal range n-term range n-term range n-terminal range n-term range colocalization colocalization Fig. 4B