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 MT1-MMP cleaves Dll1 to negatively regulate Notch signalling to maintain normal B-cell development. MT1-MMP cleaves Dll1 to negatively regulate Notch signalling to maintain normal B-cell development. EMBO J. (0261-4189) 2011 imex curation Jin G., Zhang F., Chan KM., Xavier Wong HL., Liu B., Cheah KS., Liu X., Mauch C., Liu D., Zhou Z. Only protein-protein interactions mouse-bmsc Mus musculus bmsc Bone Marrow Stromal cells anti bait coip anti bait coimmunoprecipitation anti bait coip western blot western blot Immuno blot Immuno blot Jin G., Zhang F., Chan KM., Xavier Wong HL., Liu B., Cheah KS., Liu X., Mauch C., Liu D., Zhou Z. EMBO J. (0261-4189) 2011 Only protein-protein interactions imex curation MT1-MMP cleaves Dll1 to negatively regulate Notch signalling to maintain normal B-cell development. MT1-MMP cleaves Dll1 to negatively regulate Notch signalling to maintain normal B-cell development. EMBO J. (0261-4189) 2011 imex curation Jin G., Zhang F., Chan KM., Xavier Wong HL., Liu B., Cheah KS., Liu X., Mauch C., Liu D., Zhou Z. Only protein-protein interactions in vitro In vitro protease assay protease assay predetermined predetermined participant predetermined Jin G., Zhang F., Chan KM., Xavier Wong HL., Liu B., Cheah KS., Liu X., Mauch C., Liu D., Zhou Z. EMBO J. (0261-4189) 2011 Only protein-protein interactions imex curation mmp14_mouse Matrix metalloproteinase-14 Mmp14 Mtmmp Membrane-type matrix metalloproteinase 1 Membrane-type-1 matrix metalloproteinase MMP-X1 MT-MMP protein protein mouse Mus musculus Mouse MSPAPRPSRSLLLPLLTLGTALASLGWAQGSNFSPEAWLQQYGYLPPGDLRTHTQRSPQSLSAAIAAMQKFYGLQVTGKADLATMMAMRRPRCGVPDKFGTEIKANVRRKRYAIQGLKWQHNEITFCIQNYTPKVGEYATFEAIRKAFRVWESATPLRFREVPYAYIREGHEKQADIMILFAEGFHGDSTPFDGEGGFLAHAYFPGPNIGGDTHFDSAEPWTVQNEDLNGNDIFLVAVHELGHALGLEHSNDPSAIMAPFYQWMDTENFVLPDDDRRGIQQLYGSKSGSPTKMPPQPRTTSRPSVPDKPKNPAYGPNICDGNFDTVAMLRGEMFVFKERWFWRVRNNQVMDGYPMPIGQFWRGLPASINTAYERKDGKFVFFKGDKHWVFDEASLEPGYPKHIKELGRGLPTDKIDAALFWMPNGKTYFFRGNKYYRFNEEFRAVDSEYPKNIKVWEGIPESPRGSFMGSDEVFTYFYKGNKYWKFNNQKLKVEPGYPKSALRDWMGCPSGGRPDEGTEEETEVIIIEVDEEGSGAVSAAAVVLPVLLLLLVLAVGLAVFFFRRHGTPKRLLYCQRSLLDKV mint Endopeptidase that degrades various components of the extracellular matrix, such as collagen. Activates progelatinase A. Essential for pericellular collagenolysis and modeling of skeletal and extraskeletal connective tissues during development 6CA95CFD5811B093 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 dll1_mouse Delta-like protein 1 Dll1 Drosophila Delta homolog 1 protein protein mouse Mus musculus Mouse MGRRSALALAVVSALLCQVWSSGVFELKLQEFVNKKGLLGNRNCCRGGSGPPCACRTFFRVCLKHYQASVSPEPPCTYGSAVTPVLGVDSFSLPDGAGIDPAFSNPIRFPFGFTWPGTFSLIIEALHTDSPDDLATENPERLISRLTTQRHLTVGEEWSQDLHSSGRTDLRYSYRFVCDEHYYGEGCSVFCRPRDDAFGHFTCGDRGEKMCDPGWKGQYCTDPICLPGCDDQHGYCDKPGECKCRVGWQGRYCDECIRYPGCLHGTCQQPWQCNCQEGWGGLFCNQDLNYCTHHKPCRNGATCTNTGQGSYTCSCRPGYTGANCELEVDECAPSPCKNGASCTDLEDSFSCTCPPGFYGKVCELSAMTCADGPCFNGGRCSDNPDGGYTCHCPLGFSGFNCEKKMDLCGSSPCSNGAKCVDLGNSYLCRCQAGFSGRYCEDNVDDCASSPCANGGTCRDSVNDFSCTCPPGYTGKNCSAPVSRCEHAPCHNGATCHQRGQRYMCECAQGYGGPNCQFLLPEPPPGPMVVDLSERHMESQGGPFPWVAVCAGVVLVLLLLLGCAAVVVCVRLKLQKHQPPPEPCGGETETMNNLANCQREKDVSVSIIGATQIKNTNKKADFHGDHGAEKSSFKVRYPTVDYNLVRDLKGDEATVRDTHSKRDTKCQSQSSAGEEKIAPTLRGGEIPDRKRPESVYSTSKDTKYQSVYVLSAEKDECVIATEV DIP protein Q61483 original sequence version: 83 9D570B9DC7EEC75E dll1-mmp14 1 MT1-MMP 3 western blot western blot Immuno blot Immuno blot predetermined predetermined participant predetermined unspecified role unspecified role prey prey physiological level physiological level endogenous level endogenous endogenous endogenous level Dll1 5 western blot western blot Immuno blot Immuno blot predetermined predetermined participant predetermined unspecified role unspecified role bait bait living cell living cell physiological level physiological level endogenous level endogenous endogenous endogenous level physical association physical association f8a homomint mint dll1-mmp14-1 2 MT1-MMP 4 predetermined predetermined participant predetermined predetermined predetermined participant predetermined enzyme enzyme neutral component neutral component purified purified binding site binding region binding-associated region binding region certain certain sequence position certain certain certain sequence position certain Dll1 5 peptide synthesis peptide synthesis predetermined predetermined participant predetermined enzyme target enzyme target substrate substrate neutral component neutral component purified purified binding site binding region binding-associated region binding region certain certain sequence position certain certain certain sequence position certain other modification other modification uncategorized protein modification uncategorized protein modification modified residue ms mass detection of residue modification modified residue ms certain certain sequence position certain certain certain sequence position certain resulting-ptm cleavage cleavage reaction cleavage sf6 homomint mint To determine if MT1-MMP cleaves Dll1 directly, we synthesized a Dll1 polypeptide (516QFLLPEP PPGPMVVDLSERHMESQGGPFP) containing ADAM10 cleavage site H-536M and incubated it with the recombinant catalytic form of MT1-MMP. Mass spectrometry analyses of the reaction products showed a fragment at 2015.9 Da (Supplementary Figure S6A). Its amino-acid sequence was further identified as 527MVVDLSERHMESQGGPFP by tandem MS/MS (Supplementary Figure S6B), suggesting that MT1-MMP can cleave Dll1 directly at P-527M.