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/ Structural basis of Smad1 activation by receptor kinase phosphorylation. Structural basis of Smad1 activation by receptor kinase phosphorylation. Mol. Cell (1097-2765) 2001 imex curation Qin B.Y., Chacko B.M., Lam S.S., de Caestecker M.P., Correia J.J., Lin K. kai.lin@umassmed.edu 26-Feb-2015: Contacted by IntAct-Help. Only protein-protein interactions in vitro In vitro molecular sieving molecular sieving Gel Filtration Size Exclusion Chromatography Size Exclusion Chromatography Gel Filtration Sizing column western blot western blot Immuno blot Immuno blot Qin B.Y., Chacko B.M., Lam S.S., de Caestecker M.P., Correia J.J., Lin K. kai.lin@umassmed.edu Accepted 2015-FEB-13 by MGT Mol. Cell (1097-2765) 2001 Only protein-protein interactions imex curation Structural basis of Smad1 activation by receptor kinase phosphorylation. Structural basis of Smad1 activation by receptor kinase phosphorylation. Mol. Cell (1097-2765) 2001 imex curation Qin B.Y., Chacko B.M., Lam S.S., de Caestecker M.P., Correia J.J., Lin K. kai.lin@umassmed.edu 26-Feb-2015: Contacted by IntAct-Help. Only protein-protein interactions in vitro In vitro x-ray diffraction x-ray crystallography X-ray X-ray x-ray diffraction predetermined predetermined participant predetermined Qin B.Y., Chacko B.M., Lam S.S., de Caestecker M.P., Correia J.J., Lin K. kai.lin@umassmed.edu Accepted 2015-FEB-13 by MGT Mol. Cell (1097-2765) 2001 Only protein-protein interactions imex curation Structural basis of Smad1 activation by receptor kinase phosphorylation. Structural basis of Smad1 activation by receptor kinase phosphorylation. Mol. Cell (1097-2765) 2001 imex curation Qin B.Y., Chacko B.M., Lam S.S., de Caestecker M.P., Correia J.J., Lin K. kai.lin@umassmed.edu 26-Feb-2015: Contacted by IntAct-Help. Only protein-protein interactions in vitro In vitro density sedimentation cosedimentation through density gradient density sedimentation predetermined predetermined participant predetermined Qin B.Y., Chacko B.M., Lam S.S., de Caestecker M.P., Correia J.J., Lin K. kai.lin@umassmed.edu Accepted 2015-FEB-13 by MGT Mol. Cell (1097-2765) 2001 Only protein-protein interactions imex curation smad1_human Mothers against decapentaplegic homolog 1 Mad-related protein 1 SMAD family member 1 Transforming growth factor-beta-signaling protein 1 JV4-1 SMAD1 BSP1 MADH1 MADR1 protein protein human Homo sapiens Human MNVTSLFSFTSPAVKRLLGWKQGDEEEKWAEKAVDALVKKLKKKKGAMEELEKALSCPGQPSNCVTIPRSLDGRLQVSHRKGLPHVIYCRVWRWPDLQSHHELKPLECCEFPFGSKQKEVCINPYHYKRVESPVLPPVLVPRHSEYNPQHSLLAQFRNLGQNEPHMPLNATFPDSFQQPNSHPFPHSPNSSYPNSPGSSSSTYPHSPTSSDPGSPFQMPADTPPPAYLPPEDPMTQDGSQPMDTNMMAPPLPSEINRGDVQAVAYEEPKHWCSIVYYELNNRVGEAFHASSTSVLVDGFTDPSNNKNRFCLGLLSNVNRNSTIENTRRHIGKGVHLYYVGGEVYAECLSDSSIFVQSRNCNYHHGFHPTTVCKIPSGCSLKIFNNQEFAQLLAQSVNHGFETVYELTKMCTIRMSFVKGWGAEYHRQDVTSTPCWIEIHLHGPLQWLDKVLTQMGSPHNPISSVS DIP protein Q15797 original sequence version: 167 DIP protein Q15797 original sequence version: 145 DIP protein Q15797 original sequence version: 133 2DD34B7F434DBC7E smad4_human Mothers against decapentaplegic homolog 4 SMAD4 DPC4 MADH4 SMAD family member 4 Deletion target in pancreatic carcinoma 4 protein protein human Homo sapiens Human MDNMSITNTPTSNDACLSIVHSLMCHRQGGESETFAKRAIESLVKKLKEKKDELDSLITAITTNGAHPSKCVTIQRTLDGRLQVAGRKGFPHVIYARLWRWPDLHKNELKHVKYCQYAFDLKCDSVCVNPYHYERVVSPGIDLSGLTLQSNAPSSMMVKDEYVHDFEGQPSLSTEGHSIQTIQHPPSNRASTETYSTPALLAPSESNATSTANFPNIPVASTSQPASILGGSHSEGLLQIASGPQPGQQQNGFTGQPATYHHNSTTTWTGSRTAPYTPNLPHHQNGHLQHHPPMPPHPGHYWPVHNELAFQPPISNHPAPEYWCSIAYFEMDVQVGETFKVPSSCPIVTVDGYVDPSGGDRFCLGQLSNVHRTEAIERARLHIGKGVQLECKGEGDVWVRCLSDHAVFVQSYYLDREAGRAPGDAVHKIYPSAYIKVFDLRQCHRQMQQQAATAQAAAAAQAAAVAGNIPGPGSVGGIAPAISLSAAAGIGVDDLRRLCILRMSFVKGWGPDYPRQSIKETPCWIEIHLHRALQLLDEVLHTMPIADPQPLD DIP protein Q13485 original sequence version: 149 DIP protein Q13485 original sequence version: 177 7EE3C4647712DA90 smad1-1 2 4 unspecified role unspecified role neutral component neutral component region sufficient to bind sufficient binding region sufficient to bind certain certain sequence position certain certain certain sequence position certain ecoli Escherichia coli (strain K12) direct interaction direct interaction Table 2 smad1-1 3 4 unspecified role unspecified role neutral component neutral component Q15797:p.Ser463Asp mutation mutation certain certain sequence position certain certain certain sequence position certain S D Wed May 02 14:27:28 BST 2018 This feature has been corrected as a result of our quality control procedures. The original label was 'ser463asp' Tue Jun 30 16:30:41 BST 2020 This feature has been corrected as a result of our quality control procedures. The original label was 'p.Ser463Asp' region sufficient to bind sufficient binding region sufficient to bind certain certain sequence position certain certain certain sequence position certain true Q15797:p.Ser465Asp mutation mutation certain certain sequence position certain certain certain sequence position certain S D Wed May 02 19:38:34 BST 2018 This feature has been corrected as a result of our quality control procedures. The original label was 'ser465asp' Tue Jun 30 17:24:51 BST 2020 This feature has been corrected as a result of our quality control procedures. The original label was 'p.Ser465Asp' ecoli Escherichia coli (strain K12) direct interaction direct interaction Fig 1A,Table 1 The pseudo-phosphorylated mutated form demonstrates a 4278-fold enhanced trimerization ability as compared to the corresponding unphosphorylated form. smad1-1 3 4 unspecified role unspecified role neutral component neutral component region sufficient to bind sufficient binding region sufficient to bind certain certain sequence position certain certain certain sequence position certain true ecoli Escherichia coli (strain K12) direct interaction direct interaction Table 1 smad1-1 1 4 unspecified role unspecified role neutral component neutral component region sufficient to bind sufficient binding region sufficient to bind certain certain sequence position certain certain certain sequence position certain true Q15797:p.Asp297His mutation disrupting strength mutation disrupting interaction strength mutation disrupting strength certain certain sequence position certain certain certain sequence position certain D H Wed May 02 16:05:55 BST 2018 This feature has been corrected as a result of our quality control procedures. The original label was 'asp297his' Tue Jun 30 16:48:44 BST 2020 This feature has been corrected as a result of our quality control procedures. The original label was 'p.Asp297His' Q15797:p.Asp448His mutation disrupting strength mutation disrupting interaction strength mutation disrupting strength certain certain sequence position certain certain certain sequence position certain D H Wed May 02 16:20:27 BST 2018 This feature has been corrected as a result of our quality control procedures. The original label was 'asp448his' Tue Jun 30 16:25:22 BST 2020 This feature has been corrected as a result of our quality control procedures. The original label was 'p.Asp448His' Q15797:p.Val317Asp mutation disrupting strength mutation disrupting interaction strength mutation disrupting strength certain certain sequence position certain certain certain sequence position certain V D Wed May 02 19:10:36 BST 2018 This feature has been corrected as a result of our quality control procedures. The original label was 'val317asp' Tue Jun 30 17:14:18 BST 2020 This feature has been corrected as a result of our quality control procedures. The original label was 'p.Val317Asp' Q15797:p.Lys373Ser mutation disrupting strength mutation disrupting interaction strength mutation disrupting strength certain certain sequence position certain certain certain sequence position certain K S Wed May 02 19:32:03 BST 2018 This feature has been corrected as a result of our quality control procedures. The original label was 'lys373ser' Tue Jun 30 19:51:27 BST 2020 This feature has been corrected as a result of our quality control procedures. The original label was 'p.Lys373Ser' Q15797:p.Lys418Ser mutation disrupting strength mutation disrupting interaction strength mutation disrupting strength certain certain sequence position certain certain certain sequence position certain K S Wed May 02 17:12:41 BST 2018 This feature has been corrected as a result of our quality control procedures. The original label was 'lys418ser' Tue Jun 30 17:11:24 BST 2020 This feature has been corrected as a result of our quality control procedures. The original label was 'p.Lys418Ser' Q15797:p.Tyr424Phe mutation decreasing strength mutation decreasing interaction strength mutation decreasing strength certain certain sequence position certain certain certain sequence position certain Y F Wed May 02 18:48:31 BST 2018 This feature has been corrected as a result of our quality control procedures. The original label was 'tyr424phe' Tue Jun 30 17:03:28 BST 2020 This feature has been corrected as a result of our quality control procedures. The original label was 'p.Tyr424Phe' Q15797:p.Arg426Ser mutation disrupting strength mutation disrupting interaction strength mutation disrupting strength certain certain sequence position certain certain certain sequence position certain R S Wed May 02 14:43:17 BST 2018 This feature has been corrected as a result of our quality control procedures. The original label was 'arg426ser' Tue Jun 30 17:06:44 BST 2020 This feature has been corrected as a result of our quality control procedures. The original label was 'p.Arg426Ser' Q15797:p.Ser463Asp mutation mutation certain certain sequence position certain certain certain sequence position certain S D Wed May 02 19:29:08 BST 2018 This feature has been corrected as a result of our quality control procedures. The original label was 'ser463asp' Tue Jun 30 16:55:03 BST 2020 This feature has been corrected as a result of our quality control procedures. The original label was 'p.Ser463Asp' Q15797:p.Ser465Asp mutation mutation certain certain sequence position certain certain certain sequence position certain S D Wed May 02 14:25:27 BST 2018 This feature has been corrected as a result of our quality control procedures. The original label was 'ser465asp' Tue Jun 30 18:55:43 BST 2020 This feature has been corrected as a result of our quality control procedures. The original label was 'p.Ser465Asp' ecoli Escherichia coli (strain K12) direct interaction direct interaction Figure 3 A/B smad1-smad4-5 1 4 unspecified role unspecified role neutral component neutral component Q15797:p.Ser463Asp mutation mutation certain certain sequence position certain certain certain sequence position certain true S D Wed May 02 19:27:29 BST 2018 This feature has been corrected as a result of our quality control procedures. The original label was 'ser463asp' Tue Jun 30 19:18:02 BST 2020 This feature has been corrected as a result of our quality control procedures. The original label was 'p.Ser463Asp' region sufficient to bind sufficient binding region sufficient to bind certain certain sequence position certain certain certain sequence position certain true Q15797:p.Ser465Asp mutation mutation certain certain sequence position certain certain certain sequence position certain true S D Wed May 02 16:15:59 BST 2018 This feature has been corrected as a result of our quality control procedures. The original label was 'ser465asp' Tue Jun 30 19:32:50 BST 2020 This feature has been corrected as a result of our quality control procedures. The original label was 'p.Ser465Asp' ecoli Escherichia coli (strain K12) 5 unspecified role unspecified role neutral component neutral component region sufficient to bind sufficient binding region sufficient to bind certain certain sequence position certain certain certain sequence position certain Q13485:p.Asp351His mutation disrupting strength mutation disrupting interaction strength mutation disrupting strength certain certain sequence position certain certain certain sequence position certain D H Wed May 02 17:33:35 BST 2018 This feature has been corrected as a result of our quality control procedures. The original label was 'asp351his' Tue Jun 30 19:46:22 BST 2020 This feature has been corrected as a result of our quality control procedures. The original label was 'p.Asp351His' Q13485:p.Asp537Glu mutation decreasing strength mutation decreasing interaction strength mutation decreasing strength certain certain sequence position certain certain certain sequence position certain D E Wed May 02 17:05:16 BST 2018 This feature has been corrected as a result of our quality control procedures. The original label was 'asp537glu' Tue Jun 30 20:19:21 BST 2020 This feature has been corrected as a result of our quality control procedures. The original label was 'p.Asp537Glu' Q13485:p.Val426Ser mutation decreasing strength mutation decreasing interaction strength mutation decreasing strength certain certain sequence position certain certain certain sequence position certain V S Wed May 02 15:30:31 BST 2018 This feature has been corrected as a result of our quality control procedures. The original label was 'val426ser' Tue Jun 30 20:23:08 BST 2020 This feature has been corrected as a result of our quality control procedures. The original label was 'p.Val426Ser' Q13485:p.Lys507Ser mutation disrupting strength mutation disrupting interaction strength mutation disrupting strength certain certain sequence position certain certain certain sequence position certain K S Wed May 02 20:20:59 BST 2018 This feature has been corrected as a result of our quality control procedures. The original label was 'lys507ser' Tue Jun 30 19:29:24 BST 2020 This feature has been corrected as a result of our quality control procedures. The original label was 'p.Lys507Ser' Q13485:p.Arg515Ser mutation disrupting strength mutation disrupting interaction strength mutation disrupting strength certain certain sequence position certain certain certain sequence position certain R S Wed May 02 17:06:11 BST 2018 This feature has been corrected as a result of our quality control procedures. The original label was 'arg515ser' Tue Jun 30 17:42:12 BST 2020 This feature has been corrected as a result of our quality control procedures. The original label was 'p.Arg515Ser' ecoli Escherichia coli (strain K12) 32 35 direct interaction direct interaction Fig 3B smad1-smad4-6 3 5 unspecified role unspecified role neutral component neutral component region sufficient to bind sufficient binding region sufficient to bind certain certain sequence position certain certain certain sequence position certain true ecoli Escherichia coli (strain K12) 4 unspecified role unspecified role neutral component neutral component region sufficient to bind sufficient binding region sufficient to bind certain certain sequence position certain certain certain sequence position certain true Q15797:p.Ser465Asp mutation mutation certain certain sequence position certain certain certain sequence position certain true S D Wed May 02 17:59:58 BST 2018 This feature has been corrected as a result of our quality control procedures. The original label was 'ser465asp' Tue Jun 30 18:14:43 BST 2020 This feature has been corrected as a result of our quality control procedures. The original label was 'p.Ser465Asp' Q15797:p.Ser463Asp mutation mutation certain certain sequence position certain certain certain sequence position certain true S D Wed May 02 19:22:07 BST 2018 This feature has been corrected as a result of our quality control procedures. The original label was 'ser463asp' Tue Jun 30 20:10:27 BST 2020 This feature has been corrected as a result of our quality control procedures. The original label was 'p.Ser463Asp' ecoli Escherichia coli (strain K12) 45 43 direct interaction direct interaction Fig 3C