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 http://mint.bio.uniroma2.it/mint rozanov-2002-1 The cytoplasmic tail peptide sequence of membrane type-1 matrix metalloproteinase (MT1-MMP) directly binds to gC1qR, a compartment-specific chaperone-like regulatory protein. in vitro In vitro pull down pull down predetermined predetermined participant predetermined Rozanov DV., Ghebrehiwet B., Ratnikov B., Monosov EZ., Deryugina EI., Strongin AY. Virus - Publications including interactions involving viral proteins FEBS Lett. (0014-5793) 2002 rozanovd-2002-1 The cytoplasmic tail peptide sequence of membrane type-1 matrix metalloproteinase (MT1-MMP) directly binds to gC1qR, a compartment-specific chaperone-like regulatory protein. in vivo in vivo coip coimmunoprecipitation co-immunoprecipitation CoIp immunoprecipitation Co-IP co-immunoprecipitation CoIp immunoprecipitation Co-IP coip predetermined predetermined participant predetermined Rozanov DV., Ghebrehiwet B., Ratnikov B., Monosov EZ., Deryugina EI., Strongin AY. Virus - Publications including interactions involving viral proteins FEBS Lett. (0014-5793) 2002 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 c1qbp_human Complement component 1 Q subcomponent-binding protein, mitochondrial C1QBP GC1QBP HABP1 SF2P32 Glycoprotein gC1qBP Hyaluronan-binding protein 1 Mitochondrial matrix protein p32 p33 ASF/SF2-associated protein p32 gC1q-R protein protein protein human Homo sapiens Human MLPLLRCVPRVLGSSVAGLRAAAPASPFRQLLQPAPRLCTRPFGLLSVRAGSERRPGLLRPRGPCACGCGCGSLHTDGDKAFVDFLSDEIKEERKIQKHKTLPKMSGGWELELNGTEAKLVRKVAGEKITVTFNINNSIPPTFDGEEEPSQGQKVEEQEPELTSTPNFVVEVIKNDDGKKALVLDCHYPEDEVGQEDEAESDIFSIREVSFQSTGESEWKDTNYTLNTDSLDWALYDHLMDFLADRGVDNTFADELVELSTALEHQEYITFLEDLKSFVKSQ mmp14-c1qbp 11809 mmp14_human 11811 unspecified role unspecified role bait bait purified purified binding site binding region binding-associated region binding region deletion analysis deletion analysis certain certain sequence position certain certain certain sequence position certain false Stoichiometry: 1.0 c1qbp_human 11812 unspecified role unspecified role prey prey purified purified Stoichiometry: 1.0 direct interaction direct interaction false false false homomint mint mmp14-c1qbp-1 11810 mmp14_human 11811 unspecified role unspecified role bait bait physiological level physiological level endogenous level endogenous endogenous endogenous level binding site binding region binding-associated region binding region deletion analysis deletion analysis certain certain sequence position certain certain certain sequence position certain false Stoichiometry: 1.0 c1qbp_human 11812 unspecified role unspecified role prey prey physiological level physiological level endogenous level endogenous endogenous endogenous level Stoichiometry: 1.0 physical association physical association false false false homomint mint