MINT MINT, Dpt of Biology, University of Rome Tor Vergata MINT http://mint.bio.uniroma2.it/mint url>http://mint.bio.uniroma2.it/mint/ https://mint.bio.uniroma2.it MINT-[0-9]+ https://mint.bio.uniroma2.it/index.php/results-interactions/?id=${ac} The Molecular INTeraction database (MINT) is a relational database designed to store interactions between biological molecules. http://mint.bio.uniroma2.it Structural and mutational analysis reveals that CTNNBL1 binds NLSs in a manner distinct from that of its closest armadillo-relative, karyopherin  Structural and mutational analysis reveals that CTNNBL1 binds NLSs in a manner distinct from that of its closest armadillo-relative, karyopherin  FEBS Lett. (0014-5793) 2013 imex curation Ganesh K., Maldegem F.V., Telerman S.B., Simpson P., Johnson C.M., Williams R.L., Neuberger M.S., Rada C. car@mrc-lmb.cam.ac.uk 13-Jan-2014: Contacted by IntAct-Help. Only protein-protein interactions in vitro In vitro itc isothermal titration calorimetry ITC ITC itc predetermined predetermined participant predetermined Ganesh K., Maldegem F.V., Telerman S.B., Simpson P., Johnson C.M., Williams R.L., Neuberger M.S., Rada C. car@mrc-lmb.cam.ac.uk Accepted 2013-NOV-07 by LUANA FEBS Lett. (0014-5793) 2013 Only protein-protein interactions imex curation Structural and mutational analysis reveals that CTNNBL1 binds NLSs in a manner distinct from that of its closest armadillo-relative, karyopherin  Structural and mutational analysis reveals that CTNNBL1 binds NLSs in a manner distinct from that of its closest armadillo-relative, karyopherin  FEBS Lett. (0014-5793) 2013 imex curation Ganesh K., Maldegem F.V., Telerman S.B., Simpson P., Johnson C.M., Williams R.L., Neuberger M.S., Rada C. car@mrc-lmb.cam.ac.uk 13-Jan-2014: Contacted by IntAct-Help. Only protein-protein interactions in vitro In vitro pull down pull down weight by comassie molecular weight estimation by coomasie staining weight by comassie Ganesh K., Maldegem F.V., Telerman S.B., Simpson P., Johnson C.M., Williams R.L., Neuberger M.S., Rada C. car@mrc-lmb.cam.ac.uk Accepted 2013-NOV-07 by LUANA FEBS Lett. (0014-5793) 2013 Only protein-protein interactions imex curation prp31_human U4/U6 small nuclear ribonucleoprotein Prp31 Pre-mRNA-processing factor 31 U4/U6 snRNP 61 kDa protein Serologically defined breast cancer antigen NY-BR-99 PRPF31 PRP31 protein protein human Homo sapiens Human MSLADELLADLEEAAEEEEGGSYGEEEEEPAIEDVQEETQLDLSGDSVKTIAKLWDSKMFAEIMMKIEEYISKQAKASEVMGPVEAAPEYRVIVDANNLTVEIENELNIIHKFIRDKYSKRFPELESLVPNALDYIRTVKELGNSLDKCKNNENLQQILTNATIMVVSVTASTTQGQQLSEEELERLEEACDMALELNASKHRIYEYVESRMSFIAPNLSIIIGASTAAKIMGVAGGLTNLSKMPACNIMLLGAQRKTLSGFSSTSVLPHTGYIYHSDIVQSLPPDLRRKAARLVAAKCTLAARVDSFHESTEGKVGYELKDEIERKFDKWQEPPPVKQVKPLPAPLDGQRKKRGGRRYRKMKERLGLTEIRKQANRMSFGEIEEDAYQEDLGFSLGHLGKSGSGRVRQTQVNEATKARISKTLQRTLQKQSVVYGGKSTIRDRSSGTASSVAFTPLQGLEIVNPQAAEKKVAEANQKYFSSMAEFLKVKGEKSGLMST 7B50EC4C3393795C ctbl1_human Beta-catenin-like protein 1 Nuclear-associated protein Testis development protein NYD-SP19 PP8304 CTNNBL1 C20orf33 protein protein human Homo sapiens Human MDVGELLSYQPNRGTKRPRDDEEEEQKMRRKQTGTRERGRYREEEMTVVEEADDDKKRLLQIIDRDGEEEEEEEEPLDESSVKKMILTFEKRSYKNQELRIKFPDNPEKFMESELDLNDIIQEMHVVATMPDLYHLLVELNAVQSLLGLLGHDNTDVSIAVVDLLQELTDIDTLHESEEGAEVLIDALVDGQVVALLVQNLERLDESVKEEADGVHNTLAIVENMAEFRPEMCTEGAQQGLLQWLLKRLKAKMPFDANKLYCSEVLAILLQDNDENRELLGELDGIDVLLQQLSVFKRHNPSTAEEQEMMENLFDSLCSCLMLSSNRERFLKGEGLQLMNLMLREKKISRSSALKVLDHAMIGPEGTDNCHKFVDILGLRTIFPLFMKSPRKIKKVGTTEKEHEEHVCSILASLLRNLRGQQRTRLLNKFTENDSEKVDRLMELHFKYLGAMQVADKKIEGEKHDMVRRGEIIDNDTEEEFYLRRLDAGLFVLQHICYIMAEICNANVPQIRQRVHQILNMRGSSIKIVRHIIKEYAENIGDGRSPEFRENEQKRILGLLENF 791BAFCEC5916B5A cdc5l_human Cell division cycle 5-like protein CDC5L Pombe cdc5-related protein KIAA0432 PCDC5RP protein protein human Homo sapiens Human MPRIMIKGGVWRNTEDEILKAAVMKYGKNQWSRIASLLHRKSAKQCKARWYEWLDPSIKKTEWSREEEEKLLHLAKLMPTQWRTIAPIIGRTAAQCLEHYEFLLDKAAQRDNEEETTDDPRKLKPGEIDPNPETKPARPDPIDMDEDELEMLSEARARLANTQGKKAKRKAREKQLEEARRLAALQKRRELRAAGIEIQKKRKRKRGVDYNAEIPFEKKPALGFYDTSEENYQALDADFRKLRQQDLDGELRSEKEGRDRKKDKQHLKRKKESDLPSAILQTSGVSEFTKKRSKLVLPAPQISDAELQEVVKVGQASEIARQTAEESGITNSASSTLLSEYNVTNNSVALRTPRTPASQDRILQEAQNLMALTNVDTPLKGGLNTPLHESDFSGVTPQRQVVQTPNTVLSTPFRTPSNGAEGLTPRSGTTPKPVINSTPGRTPLRDKLNINPEDGMADYSDPSYVKQMERESREHLRLGLLGLPAPKNDFEIVLPENAEKELEEREIDDTYIEDAADVDARKQAIRDAERVKEMKRMHKAVQKDLPRPSEVNETILRPLNVEPPLTDLQKSEELIKKEMITMLHYDLLHHPYEPSGNKKGKTVGFGTNNSEHITYLEHNPYEKFSKEELKKAQDVLVQEMEVVKQGMSHGELSSEAYNQVWEECYSQVLYLPGQSRYTRANLASKKDRIESLEKRLEINRGHMTTEAKRAAKMEKKMKILLGGYQSRAMGLMKQLNDLWDQIEQAHLELRTFEELKKHEDSAIPRRLECLKEDVQRQQEREKELQHRYADLLLEKETLKSKF DIP protein Q99459 original sequence version: 121 3390F91EE7E79DA6 cdc5l-ctnnbl1-2 1 CDC5L NLS3 5 predetermined predetermined participant predetermined predetermined predetermined participant predetermined unspecified role unspecified role neutral component neutral component purified purified binding region binding region binding-associated region binding region certain certain sequence position certain certain certain sequence position certain CTNNBL1 4 predetermined predetermined participant predetermined predetermined predetermined participant predetermined unspecified role unspecified role neutral component neutral component purified purified binding region binding region binding-associated region binding region certain certain sequence position certain certain certain sequence position certain direct interaction direct interaction f4b sf5 Multiple mutants of CTNNBL1 were also generated that carried amino acid substitutions in the putative NLS recognition groove (Figure 4A). Strikingly, all mutants retained the ability to interact with the CDC5L NLS3 as judged by a pulldown assay (Figure 4C). Indeed, not only was NLS binding retained by these mutants, but the affinity of binding to the CDC5L NLS3 (as well as to the Prp31 NLS) peptide, as monitored by ITC, was little affected by these amino acid changes; the small differences in binding affinity, such as the deletion mutant K1, might reflect a minor influence on the stability of the protein (Supplementary Figure 5). ctnnbl1-prpf31-1 1 Prp31 NLS 3 predetermined predetermined participant predetermined predetermined predetermined participant predetermined unspecified role unspecified role neutral component neutral component purified purified binding region binding region binding-associated region binding region certain certain sequence position certain certain certain sequence position certain CTNNBL1 4 predetermined predetermined participant predetermined predetermined predetermined participant predetermined unspecified role unspecified role neutral component neutral component purified purified binding region binding region binding-associated region binding region certain certain sequence position certain certain certain sequence position certain direct interaction direct interaction f4b cdc5l-ctnnbl1-1 2 CDC5L NLS3 5 weight by comassie molecular weight estimation by coomasie staining weight by comassie weight by comassie molecular weight estimation by coomasie staining weight by comassie unspecified role unspecified role prey prey purified purified gst tag gst tag glutathione s tranferase tag glutathione S-tranferase tag glutathione S-tranferase tag gst tag undetermined undetermined sequence position undetermined undetermined undetermined sequence position undetermined CTNNBL1 4 weight by comassie molecular weight estimation by coomasie staining weight by comassie weight by comassie molecular weight estimation by coomasie staining weight by comassie unspecified role unspecified role bait bait purified purified binding region binding region binding-associated region binding region certain certain sequence position certain certain certain sequence position certain his tag his tag his tag Hexa-His-tag 6-His-tag Histidine-tag Hexa-His-tag Histidine-tag 6-His-tag undetermined undetermined sequence position undetermined undetermined undetermined sequence position undetermined direct interaction direct interaction f4c Multiple mutants of CTNNBL1 were also generated that carried amino acid substitutions in the putative NLS recognition groove (Figure 4A). Strikingly, all mutants retained the ability to interact with the CDC5L NLS3 as judged by a pulldown assay (Figure 4C).