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 TDP-35 sequesters TDP-43 into cytoplasmic inclusions through binding with RNA. TDP-35 sequesters TDP-43 into cytoplasmic inclusions through binding with RNA. FEBS letters 2015 imex curation Che MX., Jiang LL., Li HY., Jiang YJ., Hu HY., Che MX., Jiang LL., Li HY., Jiang YJ., Hu HY. hyhu@sibcb.ac.cn 21-10-2015: Contacted by IntAct-Help. Only protein-protein interactions imex curation 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 anti tag western anti tag western blot anti tag western Che MX., Jiang LL., Li HY., Jiang YJ., Hu HY., Che MX., Jiang LL., Li HY., Jiang YJ., Hu HY. hyhu@sibcb.ac.cn Accepted 2015-SEP-30 AT 10:30 BST AT 10:30 BST by LUANA FEBS letters 2015 Only protein-protein interactions imex curation imex curation tadbp_human TAR DNA-binding protein 43 TARDBP TDP43 protein protein human Homo sapiens Human MSEYIRVTEDENDEPIEIPSEDDGTVLLSTVTAQFPGACGLRYRNPVSQCMRGVRLVEGILHAPDAGWGNLVYVVNYPKDNKRKMDETDASSAVKVKRAVQKTSDLIVLGLPWKTTEQDLKEYFSTFGEVLMVQVKKDLKTGHSKGFGFVRFTEYETQVKVMSQRHMIDGRWCDCKLPNSKQSQDEPLRSRKVFVGRCTEDMTEDELREFFSQYGDVMDVFIPKPFRAFAFVTFADDQIAQSLCGEDLIIKGISVHISNAEPKHNSNRQLERSGRFGGNPGGFGNQGGFGNSRGGGAGLGNNQGSNMGGGMNFGAFSINPAMMAAAQAALQSSWGMMGMLASQQNQSGPSGNNQNQGNMQREPNQAFGSGNNSYSGSNSGAAIGWGSASNAGSGSGFNGGFGSSMDSKSSGWGM DIP protein Q13148 original sequence version: 147 DIP protein Q13148 original sequence version: 114 DIP protein Q13148-1 original sequence version: 169 DIP protein Q13148-1 original sequence version: 124 8E09A1206FB4EF4A 1-73 1 2 unspecified role unspecified role bait bait over-expressed over expressed level over-expressed living cell living cell flag tag 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 binding region binding region binding-associated region binding region certain certain sequence position certain certain certain sequence position certain 2 unspecified role unspecified role prey prey over-expressed over expressed level over-expressed living cell living cell ha tag ha tag ha tag YPYDVPDYA epitope tag YPYDVPDYA epitope tag undetermined undetermined sequence position undetermined undetermined undetermined sequence position undetermined physical association physical association f1a tardbp-tardbp-6 1 2 unspecified role unspecified role bait bait over-expressed over expressed level over-expressed living cell living cell Q13148:p.[Phe147Leu;Phe149Leu] mutation decreasing mutation decreasing interaction hotspot hotspot mutation decreasing certain certain sequence position certain certain certain sequence position certain F L certain certain sequence position certain certain certain sequence position certain F L Fri Jul 22 10:53:24 BST 2016 This feature has been corrected as a result of our quality control procedures. The original label was 'phe149lue_phe147leu' Wed May 02 18:53:28 BST 2018 This feature has been corrected as a result of our quality control procedures. The original label was 'phe147leu,phe149leu' Tue Jun 30 17:47:59 BST 2020 This feature has been corrected as a result of our quality control procedures. The original label was 'p.[Phe147Leu;Phe149Leu]' flag tag 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 binding region binding region binding-associated region binding region certain certain sequence position certain certain certain sequence position certain Q13148:p.[Phe147Leu;Phe149Leu;Phe229Leu;Phe231Leu] mutation disrupting mutation disrupting interaction mutation disrupting certain certain sequence position certain certain certain sequence position certain F L certain certain sequence position certain certain certain sequence position certain F L certain certain sequence position certain certain certain sequence position certain F L certain certain sequence position certain certain certain sequence position certain F L Fri Jul 22 11:06:00 BST 2016 This feature has been corrected as a result of our quality control procedures. The original label was 'phe229leu_phe213leu_phe149lue_phe147leu' Wed May 02 19:45:35 BST 2018 This feature has been corrected as a result of our quality control procedures. The original label was 'phe147leu,phe149leu,phe229leu,phe231leu' Tue Jun 30 20:01:24 BST 2020 This feature has been corrected as a result of our quality control procedures. The original label was 'p.[Phe147Leu;Phe149Leu;Phe229Leu;Phe231Leu]' 2 unspecified role unspecified role prey prey living cell living cell physiological level physiological level endogenous level endogenous endogenous endogenous level physical association physical association f1b f1c f1d f2b We also tested whether TDP-35 associates with endogenous TDP-43. The data exhibited that FLAG-TDP-35 could immunoprecipitate the endogenous TDP-43. The restoration experiments by adding ssDNA in the RNase-A treated sample suggested that single-strand DNA could improve the association of TDP-35 with TDP-43 (Fig. 1c, lane 5), but it failed to act on TDP-25A with TDP-43 (Fig. 1c, lane 11). To test whether DNA was involved in the association, we conducted immunoprecipitation on the cell lysates treated with deoxyribonuclease (DNase). Compared with RNase-A treatment, DNase treatment did not affect sequestration of TDP-43 by TDP-35 inclusions (Fig. 1d, lane 8). Altogether, these results demonstrate that sequestration of full-length TDP-43 by the cytoplasmic TDP-35 inclusions is mediated by RNA.