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/ Furin Functions as a Nonproteolytic Chaperone for Matrix Metalloproteinase-28: MMP-28 Propeptide Sequence Requirement. Furin Functions as a Nonproteolytic Chaperone for Matrix Metalloproteinase-28: MMP-28 Propeptide Sequence Requirement. Biochemistry research international 2010 imex curation Pavlaki M., Zucker S., Dufour A., Calabrese N., Bahou W., Cao J., Pavlaki M., Zucker S., Dufour A., Calabrese N., Bahou W., Cao J. Also as data-processing comment: From PMID 2251280 cited in ref 32: Furin is of human origin and the active site mutant S/A was constructed by substituting the activesite serine residue 368 to an alanine. From ref 24: MMP28 is of human origin and c-terminally myc tagged. From ref 45: MT1-MMP s of human origin. According to IMEx curation standard interactions involving chimeric proteins and in vivo enzymatic assays were not captured. From PMID 2251280 cited in ref 32: Furin is of human origin and the active site mutant S/A was constructed by substituting the activesite serine residue 368 to an alanine. From ref 24: MMP28 is of human origin and c-terminally myc tagged. From ref 45: MT1-MMP s of human origin. According to IMEx curation standard interactions involving chimeric proteins and in vivo enzymatic assays were not captured. jicao@notes.cc.stonybrook.edu 09-May-2019: Contacted by IntAct-Help. Only protein-protein interactions imex curation chlae-cos_1 Chlorocebus aethiops COS-1 cells Grivet cos_1 CV-1 Simian cells (cercopithecus aethiops) transformed by SV40 confocal microscopy confocal microscopy immunocytochemistry immunocytochemistry Pavlaki M., Zucker S., Dufour A., Calabrese N., Bahou W., Cao J., Pavlaki M., Zucker S., Dufour A., Calabrese N., Bahou W., Cao J. Also as data-processing comment: From PMID 2251280 cited in ref 32: Furin is of human origin and the active site mutant S/A was constructed by substituting the activesite serine residue 368 to an alanine. From ref 24: MMP28 is of human origin and c-terminally myc tagged. From ref 45: MT1-MMP s of human origin. According to IMEx curation standard interactions involving chimeric proteins and in vivo enzymatic assays were not captured. From PMID 2251280 cited in ref 32: Furin is of human origin and the active site mutant S/A was constructed by substituting the activesite serine residue 368 to an alanine. From ref 24: MMP28 is of human origin and c-terminally myc tagged. From ref 45: MT1-MMP s of human origin. According to IMEx curation standard interactions involving chimeric proteins and in vivo enzymatic assays were not captured. jicao@notes.cc.stonybrook.edu Accepted 2019-JAN-17 AT 14:01 GMT AT 14:01 GMT by PPORRAS Biochemistry research international 2010 imex curation Furin Functions as a Nonproteolytic Chaperone for Matrix Metalloproteinase-28: MMP-28 Propeptide Sequence Requirement. Furin Functions as a Nonproteolytic Chaperone for Matrix Metalloproteinase-28: MMP-28 Propeptide Sequence Requirement. Biochemistry research international 2010 imex curation Pavlaki M., Zucker S., Dufour A., Calabrese N., Bahou W., Cao J., Pavlaki M., Zucker S., Dufour A., Calabrese N., Bahou W., Cao J. Also as data-processing comment: From PMID 2251280 cited in ref 32: Furin is of human origin and the active site mutant S/A was constructed by substituting the activesite serine residue 368 to an alanine. From ref 24: MMP28 is of human origin and c-terminally myc tagged. From ref 45: MT1-MMP s of human origin. According to IMEx curation standard interactions involving chimeric proteins and in vivo enzymatic assays were not captured. From PMID 2251280 cited in ref 32: Furin is of human origin and the active site mutant S/A was constructed by substituting the activesite serine residue 368 to an alanine. From ref 24: MMP28 is of human origin and c-terminally myc tagged. From ref 45: MT1-MMP s of human origin. According to IMEx curation standard interactions involving chimeric proteins and in vivo enzymatic assays were not captured. jicao@notes.cc.stonybrook.edu 09-May-2019: Contacted by IntAct-Help. Only protein-protein interactions imex curation chlae-cos_1 Chlorocebus aethiops COS-1 cells Grivet cos_1 CV-1 Simian cells (cercopithecus aethiops) transformed by SV40 anti bait coip anti bait coimmunoprecipitation anti bait coip western blot western blot Immuno blot Immuno blot Pavlaki M., Zucker S., Dufour A., Calabrese N., Bahou W., Cao J., Pavlaki M., Zucker S., Dufour A., Calabrese N., Bahou W., Cao J. Also as data-processing comment: From PMID 2251280 cited in ref 32: Furin is of human origin and the active site mutant S/A was constructed by substituting the activesite serine residue 368 to an alanine. From ref 24: MMP28 is of human origin and c-terminally myc tagged. From ref 45: MT1-MMP s of human origin. According to IMEx curation standard interactions involving chimeric proteins and in vivo enzymatic assays were not captured. From PMID 2251280 cited in ref 32: Furin is of human origin and the active site mutant S/A was constructed by substituting the activesite serine residue 368 to an alanine. From ref 24: MMP28 is of human origin and c-terminally myc tagged. From ref 45: MT1-MMP s of human origin. According to IMEx curation standard interactions involving chimeric proteins and in vivo enzymatic assays were not captured. jicao@notes.cc.stonybrook.edu Accepted 2019-JAN-17 AT 14:01 GMT AT 14:01 GMT by PPORRAS Biochemistry research international 2010 imex curation Furin Functions as a Nonproteolytic Chaperone for Matrix Metalloproteinase-28: MMP-28 Propeptide Sequence Requirement. Furin Functions as a Nonproteolytic Chaperone for Matrix Metalloproteinase-28: MMP-28 Propeptide Sequence Requirement. Biochemistry research international 2010 imex curation Pavlaki M., Zucker S., Dufour A., Calabrese N., Bahou W., Cao J., Pavlaki M., Zucker S., Dufour A., Calabrese N., Bahou W., Cao J. Also as data-processing comment: From PMID 2251280 cited in ref 32: Furin is of human origin and the active site mutant S/A was constructed by substituting the activesite serine residue 368 to an alanine. From ref 24: MMP28 is of human origin and c-terminally myc tagged. From ref 45: MT1-MMP s of human origin. According to IMEx curation standard interactions involving chimeric proteins and in vivo enzymatic assays were not captured. From PMID 2251280 cited in ref 32: Furin is of human origin and the active site mutant S/A was constructed by substituting the activesite serine residue 368 to an alanine. From ref 24: MMP28 is of human origin and c-terminally myc tagged. From ref 45: MT1-MMP s of human origin. According to IMEx curation standard interactions involving chimeric proteins and in vivo enzymatic assays were not captured. jicao@notes.cc.stonybrook.edu 09-May-2019: Contacted by IntAct-Help. Only protein-protein interactions imex curation chlae-cos_1 Chlorocebus aethiops COS-1 cells Grivet cos_1 CV-1 Simian cells (cercopithecus aethiops) transformed by SV40 anti bait coip anti bait coimmunoprecipitation anti bait coip anti tag western anti tag western blot anti tag western Pavlaki M., Zucker S., Dufour A., Calabrese N., Bahou W., Cao J., Pavlaki M., Zucker S., Dufour A., Calabrese N., Bahou W., Cao J. Also as data-processing comment: From PMID 2251280 cited in ref 32: Furin is of human origin and the active site mutant S/A was constructed by substituting the activesite serine residue 368 to an alanine. From ref 24: MMP28 is of human origin and c-terminally myc tagged. From ref 45: MT1-MMP s of human origin. According to IMEx curation standard interactions involving chimeric proteins and in vivo enzymatic assays were not captured. From PMID 2251280 cited in ref 32: Furin is of human origin and the active site mutant S/A was constructed by substituting the activesite serine residue 368 to an alanine. From ref 24: MMP28 is of human origin and c-terminally myc tagged. From ref 45: MT1-MMP s of human origin. According to IMEx curation standard interactions involving chimeric proteins and in vivo enzymatic assays were not captured. jicao@notes.cc.stonybrook.edu Accepted 2019-JAN-17 AT 14:01 GMT AT 14:01 GMT by PPORRAS Biochemistry research international 2010 imex curation Furin Functions as a Nonproteolytic Chaperone for Matrix Metalloproteinase-28: MMP-28 Propeptide Sequence Requirement. Furin Functions as a Nonproteolytic Chaperone for Matrix Metalloproteinase-28: MMP-28 Propeptide Sequence Requirement. Biochemistry research international 2010 imex curation Pavlaki M., Zucker S., Dufour A., Calabrese N., Bahou W., Cao J., Pavlaki M., Zucker S., Dufour A., Calabrese N., Bahou W., Cao J. Also as data-processing comment: From PMID 2251280 cited in ref 32: Furin is of human origin and the active site mutant S/A was constructed by substituting the activesite serine residue 368 to an alanine. From ref 24: MMP28 is of human origin and c-terminally myc tagged. From ref 45: MT1-MMP s of human origin. According to IMEx curation standard interactions involving chimeric proteins and in vivo enzymatic assays were not captured. From PMID 2251280 cited in ref 32: Furin is of human origin and the active site mutant S/A was constructed by substituting the activesite serine residue 368 to an alanine. From ref 24: MMP28 is of human origin and c-terminally myc tagged. From ref 45: MT1-MMP s of human origin. According to IMEx curation standard interactions involving chimeric proteins and in vivo enzymatic assays were not captured. jicao@notes.cc.stonybrook.edu 09-May-2019: Contacted by IntAct-Help. Only protein-protein interactions imex curation chlae-cos_1 Chlorocebus aethiops COS-1 cells Grivet cos_1 CV-1 Simian cells (cercopithecus aethiops) transformed by SV40 anti tag coip anti tag coimmunoprecipitation anti tag coip western blot western blot Immuno blot Immuno blot Pavlaki M., Zucker S., Dufour A., Calabrese N., Bahou W., Cao J., Pavlaki M., Zucker S., Dufour A., Calabrese N., Bahou W., Cao J. Also as data-processing comment: From PMID 2251280 cited in ref 32: Furin is of human origin and the active site mutant S/A was constructed by substituting the activesite serine residue 368 to an alanine. From ref 24: MMP28 is of human origin and c-terminally myc tagged. From ref 45: MT1-MMP s of human origin. According to IMEx curation standard interactions involving chimeric proteins and in vivo enzymatic assays were not captured. From PMID 2251280 cited in ref 32: Furin is of human origin and the active site mutant S/A was constructed by substituting the activesite serine residue 368 to an alanine. From ref 24: MMP28 is of human origin and c-terminally myc tagged. From ref 45: MT1-MMP s of human origin. According to IMEx curation standard interactions involving chimeric proteins and in vivo enzymatic assays were not captured. jicao@notes.cc.stonybrook.edu Accepted 2019-JAN-17 AT 14:01 GMT AT 14:01 GMT by PPORRAS Biochemistry research international 2010 imex curation furin_human Furin FURIN FUR PACE PCSK3 Paired basic amino acid residue-cleaving enzyme Dibasic-processing enzyme protein protein human Homo sapiens Human MELRPWLLWVVAATGTLVLLAADAQGQKVFTNTWAVRIPGGPAVANSVARKHGFLNLGQIFGDYYHFWHRGVTKRSLSPHRPRHSRLQREPQVQWLEQQVAKRRTKRDVYQEPTDPKFPQQWYLSGVTQRDLNVKAAWAQGYTGHGIVVSILDDGIEKNHPDLAGNYDPGASFDVNDQDPDPQPRYTQMNDNRHGTRCAGEVAAVANNGVCGVGVAYNARIGGVRMLDGEVTDAVEARSLGLNPNHIHIYSASWGPEDDGKTVDGPARLAEEAFFRGVSQGRGGLGSIFVWASGNGGREHDSCNCDGYTNSIYTLSISSATQFGNVPWYSEACSSTLATTYSSGNQNEKQIVTTDLRQKCTESHTGTSASAPLAAGIIALTLEANKNLTWRDMQHLVVQTSKPAHLNANDWATNGVGRKVSHSYGYGLLDAGAMVALAQNWTTVAPQRKCIIDILTEPKDIGKRLEVRKTVTACLGEPNHITRLEHAQARLTLSYNRRGDLAIHLVSPMGTRSTLLAARPHDYSADGFNDWAFMTTHSWDEDPSGEWVLEIENTSEANNYGTLTKFTLVLYGTAPEGLPVPPESSGCKTLTSSQACVVCEEGFSLHQKSCVQHCPPGFAPQVLDTHYSTENDVETIRASVCAPCHASCATCQGPALTDCLSCPSHASLDPVEQTCSRQSQSSRESPPQQQPPRLPPEVEAGQRLRAGLLPSHLPEVVAGLSCAFIVLVFVTVFLVLQLRSGFSFRGVKVYTMDRGLISYKGLPPEAWQEECPSDSEEDEGRGERTAFIKDQSAL DIP protein P09958 original sequence version: 107 10C44DD5892EF85D mmp14_human Matrix metalloproteinase-14 Membrane-type matrix metalloproteinase 1 Membrane-type-1 matrix metalloproteinase MMP-X1 MMP14 protein protein human Homo sapiens Human MSPAPRPPRCLLLPLLTLGTALASLGSAQSSSFSPEAWLQQYGYLPPGDLRTHTQRSPQSLSAAIAAMQKFYGLQVTGKADADTMKAMRRPRCGVPDKFGAEIKANVRRKRYAIQGLKWQHNEITFCIQNYTPKVGEYATYEAIRKAFRVWESATPLRFREVPYAYIREGHEKQADIMIFFAEGFHGDSTPFDGEGGFLAHAYFPGPNIGGDTHFDSAEPWTVRNEDLNGNDIFLVAVHELGHALGLEHSSDPSAIMAPFYQWMDTENFVLPDDDRRGIQQLYGGESGFPTKMPPQPRTTSRPSVPDKPKNPTYGPNICDGNFDTVAMLRGEMFVFKERWFWRVRNNQVMDGYPMPIGQFWRGLPASINTAYERKDGKFVFFKGDKHWVFDEASLEPGYPKHIKELGRGLPTDKIDAALFWMPNGKTYFFRGNKYYRFNEELRAVDSEYPKNIKVWEGIPESPRGSFMGSDEVFTYFYKGNKYWKFNNQKLKVEPGYPKSALRDWMGCPSGGRPDEGTEEETEVIIIEVDEEGGGAVSAAAVVLPVLLLLLVLAVGLAVFFFRRHGTPRRLLYCQRSLLDKV DIP protein P50281 original sequence version: 121 3722DE286A4BBCDE mmp28_human Matrix metalloproteinase-28 Epilysin MMP28 MMP25 UNQ1893/PRO4339 protein protein human Homo sapiens Human MVARVGLLLRALQLLLWGHLDAQPAERGGQELRKEAEAFLEKYGYLNEQVPKAPTSTRFSDAIRAFQWVSQLPVSGVLDRATLRQMTRPRCGVTDTNSYAAWAERISDLFARHRTKMRRKKRFAKQGNKWYKQHLSYRLVNWPEHLPEPAVRGAVRAAFQLWSNVSALEFWEAPATGPADIRLTFFQGDHNDGLGNAFDGPGGALAHAFLPRRGEAHFDQDERWSLSRRRGRNLFVVLAHEIGHTLGLTHSPAPRALMAPYYKRLGRDALLSWDDVLAVQSLYGKPLGGSVAVQLPGKLFTDFETWDSYSPQGRRPETQGPKYCHSSFDAITVDRQQQLYIFKGSHFWEVAADGNVSEPRPLQERWVGLPPNIEAAAVSLNDGDFYFFKGGRCWRFRGPKPVWGLPQLCRAGGLPRHPDAALFFPPLRRLILFKGARYYVLARGGLQVEPYYPRSLQDWGGIPEEVSGALPRPDGSIIFFRDDRYWRLDQAKLQATTSGRWATELPWMGCWHANSGSALF mmp28-furin-1 4 5 unspecified role unspecified role prey prey over-expressed over expressed level over-expressed living cell living cell P09958:p.Ser368Ala mutation with no effect mutation with no effect mutation with no effect mutation not affecting interaction certain certain sequence position certain certain certain sequence position certain S A Tue Jun 30 19:57:18 BST 2020 This feature has been corrected as a result of our quality control procedures. The original label was 'p.Ser368Ala' 7 anti tag western anti tag western blot anti tag western western blot western blot Immuno blot Immuno blot unspecified role unspecified role bait bait over-expressed over expressed level over-expressed living cell living cell myc tag myc tag myc tag EUKLISEED epitope tag EUKLISEED epitope tag c-term range C-terminal range c-term range c-term range C-terminal range c-term range Q9H239:p.Glu241Ala mutation with no effect mutation with no effect mutation with no effect mutation not affecting interaction certain certain sequence position certain certain certain sequence position certain E A Tue Jun 30 19:43:21 BST 2020 This feature has been corrected as a result of our quality control procedures. The original label was 'p.Glu241Ala' Q9H239:p.Arg119_Lys120delinsAlaAla mutation with no effect mutation with no effect mutation with no effect mutation not affecting interaction certain certain sequence position certain certain certain sequence position certain RK AA Tue Jun 30 16:25:53 BST 2020 This feature has been corrected as a result of our quality control procedures. The original label was 'p.Arg119_Lys120delinsAlaAla' Q9H239:p.Tyr43_Gly44delinsAlaAla mutation with no effect mutation with no effect mutation with no effect mutation not affecting interaction certain certain sequence position certain certain certain sequence position certain YG AA Tue Jun 30 17:51:50 BST 2020 This feature has been corrected as a result of our quality control procedures. The original label was 'p.Tyr43_Gly44delinsAlaAla' Q9H239:p.Tyr45_Leu46delinsAlaAla mutation disrupting strength mutation disrupting interaction strength mutation disrupting strength certain certain sequence position certain certain certain sequence position certain YL AA Tue Jun 30 16:50:25 BST 2020 This feature has been corrected as a result of our quality control procedures. The original label was 'p.Tyr45_Leu46delinsAlaAla' physical association physical association Fig. 4A, Fig. 5B mmp28-furin-2 3 5 unspecified role unspecified role bait bait over-expressed over expressed level over-expressed living cell living cell P09958:p.Ser368Ala mutation with no effect mutation with no effect mutation with no effect mutation not affecting interaction certain certain sequence position certain certain certain sequence position certain S A Tue Jun 30 19:06:38 BST 2020 This feature has been corrected as a result of our quality control procedures. The original label was 'p.Ser368Ala' 7 unspecified role unspecified role prey prey over-expressed over expressed level over-expressed living cell living cell myc tag myc tag myc tag EUKLISEED epitope tag EUKLISEED epitope tag c-term range C-terminal range c-term range c-term range C-terminal range c-term range physical association physical association Fig. 4B furin-mmp28-1 3 6 unspecified role unspecified role prey prey over-expressed over expressed level over-expressed living cell living cell myc tag myc tag myc tag EUKLISEED epitope tag EUKLISEED epitope tag undetermined undetermined sequence position undetermined undetermined undetermined sequence position undetermined 5 unspecified role unspecified role bait bait over-expressed over expressed level over-expressed living cell living cell physical association physical association Fig. 4B positive control mmp28-furin-3 1 5 unspecified role unspecified role neutral component neutral component over-expressed over expressed level over-expressed fixed cell fixed cell 7 unspecified role unspecified role neutral component neutral component over-expressed over expressed level over-expressed fixed cell fixed cell myc tag myc tag myc tag EUKLISEED epitope tag EUKLISEED epitope tag c-term range C-terminal range c-term range c-term range C-terminal range c-term range colocalization colocalization Fig. 4C furin-mmp14-1 2 6 unspecified role unspecified role bait bait over-expressed over expressed level over-expressed living cell living cell region required to bind necessary binding region required to bind deletion analysis deletion analysis range range range range 5 unspecified role unspecified role prey prey over-expressed over expressed level over-expressed living cell living cell physical association physical association Fig. 5A positive control