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 Pigment epithelium-derived factor binds to cell-surface F(1)-ATP synthase. Pigment epithelium-derived factor binds to cell-surface F(1)-ATP synthase. FEBS J. (1742-464X) 2010 imex curation Notari L., Arakaki N., Mueller D., Meier S., Amaral J., Becerra SP. Only protein-protein interactions in vitro In vitro competition binding competition binding predetermined predetermined participant predetermined Notari L., Arakaki N., Mueller D., Meier S., Amaral J., Becerra SP. FEBS J. (1742-464X) 2010 Only protein-protein interactions imex curation Pigment epithelium-derived factor binds to cell-surface F(1)-ATP synthase. Pigment epithelium-derived factor binds to cell-surface F(1)-ATP synthase. FEBS J. (1742-464X) 2010 imex curation Notari L., Arakaki N., Mueller D., Meier S., Amaral J., Becerra SP. Only protein-protein interactions in vitro In vitro molecular sieving molecular sieving Gel Filtration Size Exclusion Chromatography Size Exclusion Chromatography Gel Filtration Sizing column predetermined predetermined participant predetermined Notari L., Arakaki N., Mueller D., Meier S., Amaral J., Becerra SP. FEBS J. (1742-464X) 2010 Only protein-protein interactions imex curation Pigment epithelium-derived factor binds to cell-surface F(1)-ATP synthase. Pigment epithelium-derived factor binds to cell-surface F(1)-ATP synthase. FEBS J. (1742-464X) 2010 imex curation Notari L., Arakaki N., Mueller D., Meier S., Amaral J., Becerra SP. Only protein-protein interactions in vitro In vitro spr surface plasmon resonance Optical biosensor BIAcore(r) BIAcore(r) Optical biosensor spr predetermined predetermined participant predetermined Notari L., Arakaki N., Mueller D., Meier S., Amaral J., Becerra SP. FEBS J. (1742-464X) 2010 Only protein-protein interactions imex curation atpb_yeast ATP synthase subunit beta, mitochondrial ATP2 J2041 YJR121W protein protein yeast Saccharomyces cerevisiae Baker's yeast MVLPRLYTATSRAAFKAAKQSAPLLSTSWKRCMASAAQSTPITGKVTAVIGAIVDVHFEQSELPAILNALEIKTPQGKLVLEVAQHLGENTVRTIAMDGTEGLVRGEKVLDTGGPISVPVGRETLGRIINVIGEPIDERGPIKSKLRKPIHADPPSFAEQSTSAEILETGIKVVDLLAPYARGGKIGLFGGAGVGKTVFIQELINNIAKAHGGFSVFTGVGERTREGNDLYREMKETGVINLEGESKVALVFGQMNEPPGARARVALTGLTIAEYFRDEEGQDVLLFIDNIFRFTQAGSEVSALLGRIPSAVGYQPTLATDMGLLQERITTTKKGSVTSVQAVYVPADDLTDPAPATTFAHLDATTVLSRGISELGIYPAVDPLDSKSRLLDAAVVGQEHYDVASKVQETLQTYKSLQDIIAILGMDELSEQDKLTVERARKIQRFLSQPFAVAEVFTGIPGKLVRLKDTVASFKAVLEGKYDNIPEHAFYMVGGIEDVVAKAEKLAAEAN EDFF256826F68F0C EDFF256826F68F0C plmn_human Plasminogen PLG protein protein human Homo sapiens Human MEHKEVVLLLLLFLKSGQGEPLDDYVNTQGASLFSVTKKQLGAGSIEECAAKCEEDEEFTCRAFQYHSKEQQCVIMAENRKSSIIIRMRDVVLFEKKVYLSECKTGNGKNYRGTMSKTKNGITCQKWSSTSPHRPRFSPATHPSEGLEENYCRNPDNDPQGPWCYTTDPEKRYDYCDILECEEECMHCSGENYDGKISKTMSGLECQAWDSQSPHAHGYIPSKFPNKNLKKNYCRNPDRELRPWCFTTDPNKRWELCDIPRCTTPPPSSGPTYQCLKGTGENYRGNVAVTVSGHTCQHWSAQTPHTHNRTPENFPCKNLDENYCRNPDGKRAPWCHTTNSQVRWEYCKIPSCDSSPVSTEQLAPTAPPELTPVVQDCYHGDGQSYRGTSSTTTTGKKCQSWSSMTPHRHQKTPENYPNAGLTMNYCRNPDADKGPWCFTTDPSVRWEYCNLKKCSGTEASVVAPPPVVLLPDVETPSEEDCMFGNGKGYRGKRATTVTGTPCQDWAAQEPHRHSIFTPETNPRAGLEKNYCRNPDGDVGGPWCYTTNPRKLYDYCDVPQCAAPSFDCGKPQVEPKKCPGRVVGGCVAHPHSWPWQVSLRTRFGMHFCGGTLISPEWVLTAAHCLEKSPRPSSYKVILGAHQEVNLEPHVQEIEVSRLFLEPTRKDIALLKLSSPAVITDKVIPACLPSPNYVVADRTECFITGWGETQGTFGAGLLKEAQLPVIENKVCNRYEFLNGRVQSTELCAGHLAGGTDSCQGDSGGPLVCFEKDKYILQGVTSWGLGCARPNKPGVYVRVSRFVTWIEGVMRNN 8B31CB877CCB3AB6 pedf_human Pigment epithelium-derived factor SERPINF1 PEDF Serpin F1 EPC-1 Cell proliferation-inducing gene 35 protein PIG35 protein protein human Homo sapiens Human MQALVLLLCIGALLGHSSCQNPASPPEEGSPDPDSTGALVEEEDPFFKVPVNKLAAAVSNFGYDLYRVRSSTSPTTNVLLSPLSVATALSALSLGAEQRTESIIHRALYYDLISSPDIHGTYKELLDTVTAPQKNLKSASRIVFEKKLRIKSSFVAPLEKSYGTRPRVLTGNPRLDLQEINNWVQAQMKGKLARSTKEIPDEISILLLGVAHFKGQWVTKFDSRKTSLEDFYLDEERTVRVPMMSDPKAVLRYGLDSDLSCKIAQLPLTGSMSIIFFLPLKVTQNLTLIEESLTSEFIHDIDRELKTVQAVLTVPKLKLSYEGEVTKSLQEMKLQSLFDSPDFSKITGKPIKLTQVEHRAGFEWNEDGAGTTPSPGLQPAHLTFPLDYHLNQPFIFVLRDTDTGALLFIGKILDPRGP 7630DD2B4026A0D3 atpg_yeast ATP synthase subunit gamma, mitochondrial ATP3 YBR039W YBR0408 F-ATPase gamma subunit ATP3a ATP3b protein protein yeast Saccharomyces cerevisiae Baker's yeast MLSRIVSNNATRSVMCHQAQVGILYKTNPVRTYATLKEVEMRLKSIKNIEKITKTMKIVASTRLSKAEKAKISAKKMDEAEQLFYKNAETKNLDVEATETGAPKELIVAITSDKGLCGSIHSQLAKAVRRHLNDQPNADIVTIGDKIKMQLLRTHPNNIKLSINGIGKDAPTFQESALIADKLLSVMKAGTYPKISIFYNDPVSSLSFEPSEKPIFNAKTIEQSPSFGKFEIDTDANVPRDLFEYTLANQMLTAMAQGYAAEISARRNAMDNASKNAGDMINRYSILYNRTRQAVITNELVDIITGASSLG ADC71F3C1E0CDF91 ADC71F3C1E0CDF91 atpa_yeast ATP synthase subunit alpha, mitochondrial ATP1 YBL0827 YBL099W protein protein yeast Saccharomyces cerevisiae Baker's yeast MLARTAAIRSLSRTLINSTKAARPAAAALASTRRLASTKAQPTEVSSILEERIKGVSDEANLNETGRVLAVGDGIARVFGLNNIQAEELVEFSSGVKGMALNLEPGQVGIVLFGSDRLVKEGELVKRTGNIVDVPVGPGLLGRVVDALGNPIDGKGPIDAAGRSRAQVKAPGILPRRSVHEPVQTGLKAVDALVPIGRGQRELIIGDRQTGKTAVALDTILNQKRWNNGSDESKKLYCVYVAVGQKRSTVAQLVQTLEQHDAMKYSIIVAATASEAAPLQYLAPFTAASIGEWFRDNGKHALIVYDDLSKQAVAYRQLSLLLRRPPGREAYPGDVFYLHSRLLERAAKLSEKEGSGSLTALPVIETQGGDVSAYIPTNVISITDGQIFLEAELFYKGIRPAINVGLSVSRVGSAAQVKALKQVAGSLKLFLAQYREVAAFAQFGSDLDASTKQTLVRGERLTQLLKQNQYSPLATEEQVPLIYAGVNGHLDGIELSRIGEFESSFLSYLKSNHNELLTEIREKGELSKELLASLKSATESFVATF E8041D289B924696 E8041D289B924696 atpd_yeast ATP synthase subunit delta, mitochondrial ATP16 YDL004W YD8119.03 D2935 F-ATPase delta subunit protein protein yeast Saccharomyces cerevisiae Baker's yeast MLRSIIGKSASRSLNFVAKRSYAEAAAASSGLKLQFALPHETLYSGSEVTQVNLPAKSGRIGVLANHVPTVEQLLPGVVEVMEGSNSKKFFISGGFATVQPDSQLCVTAIEAFPLESFSQENIKNLLAEAKKNVSSSDAREAAEAAIQVEVLENLQSVLK mint Mitochondrial membrane ATP synthase (F(1)F(O) ATP synthase or Complex V) produces ATP from ADP in the presence of a proton gradient across the membrane which is generated by electron transport complexes of the respiratory chain. F-type ATPases consist of two structural domains, F(1) - containing the extramembraneous catalytic core, and F(0) - containing the membrane proton channel, linked together by a central stalk and a peripheral stalk. During catalysis, ATP turnover in the catalytic domain of F(1) is coupled via a rotary mechanism of the central stalk subunits to proton translocation. Part of the complex F(1) domain and of the central stalk which is part of the complex rotary element. Rotation of the central stalk against the surrounding alpha(3)beta(3) subunits leads to hydrolysis of ATP in three separate catalytic sites on the beta subunits AE8D0BA364107977 atp5e_yeast ATP synthase subunit epsilon, mitochondrial ATP15 P0345 YPL271W protein protein yeast Saccharomyces cerevisiae Baker's yeast MSAWRKAGISYAAYLNVAAQAIRSSLKTELQTASVLNRSQTDAFYTQYKNGTAASEPTPITK 0CD754A9DEFFD08C atp1-atp2-1 2 F-ATPase gamma subunit 7 weight by staining molecular weight estimation by staining weight by staining predetermined predetermined participant predetermined unspecified role unspecified role neutral component neutral component purified purified F-ATPase alpha subunit 8 weight by staining molecular weight estimation by staining weight by staining predetermined predetermined participant predetermined unspecified role unspecified role neutral component neutral component purified purified PEDF 6 monoclonal western monoclonal antibody western blot monoclonal western predetermined predetermined participant predetermined unspecified role unspecified role neutral component neutral component purified purified F-ATPase beta subunit 4 weight by staining molecular weight estimation by staining weight by staining predetermined predetermined participant predetermined unspecified role unspecified role neutral component neutral component purified purified his tag his tag his tag Hexa-His-tag 6-His-tag Histidine-tag Hexa-His-tag Histidine-tag 6-His-tag undetermined undetermined sequence position undetermined undetermined undetermined sequence position undetermined physical association physical association f1 homomint mint The F1 domain is composed of nine polypeptides with the stoichiometry α3β3γδε with a molecular weight of 370 kDa atp1-atp15 2 F-ATPase delta subunit 9 weight by staining molecular weight estimation by staining weight by staining predetermined predetermined participant predetermined unspecified role unspecified role neutral component neutral component purified purified PEDF 6 weight by staining molecular weight estimation by staining weight by staining predetermined predetermined participant predetermined unspecified role unspecified role neutral component neutral component purified purified fluorescent prot tag fluorescent prot tag fluorescent protein tag fluorescent prot tag undetermined undetermined sequence position undetermined undetermined undetermined sequence position undetermined F-ATPase gamma subunit 7 weight by staining molecular weight estimation by staining weight by staining predetermined predetermined participant predetermined unspecified role unspecified role neutral component neutral component purified purified F-ATPase epsilon subunit 10 weight by staining molecular weight estimation by staining weight by staining predetermined predetermined participant predetermined unspecified role unspecified role neutral component neutral component purified purified F-ATPase beta subunit 4 weight by staining molecular weight estimation by staining weight by staining predetermined predetermined participant predetermined unspecified role unspecified role neutral component neutral component purified purified his tag his tag his tag Hexa-His-tag 6-His-tag Histidine-tag Hexa-His-tag Histidine-tag 6-His-tag undetermined undetermined sequence position undetermined undetermined undetermined sequence position undetermined F-ATPase alpha subunit 8 weight by staining molecular weight estimation by staining weight by staining predetermined predetermined participant predetermined unspecified role unspecified role neutral component neutral component purified purified physical association physical association homomint mint The F1 domain is composed of nine polypeptides with the stoichiometry α3β3γδε with a molecular weight of 370 kDa fs3 serpinf1-atp1 3 F-ATPase delta subunit 9 predetermined predetermined participant predetermined predetermined predetermined participant predetermined unspecified role unspecified role prey prey purified purified F-ATPase epsilon subunit 10 predetermined predetermined participant predetermined predetermined predetermined participant predetermined unspecified role unspecified role prey prey purified purified F-ATPase alpha subunit 8 predetermined predetermined participant predetermined predetermined predetermined participant predetermined unspecified role unspecified role prey prey purified purified F-ATPase gamma subunit 7 predetermined predetermined participant predetermined predetermined predetermined participant predetermined unspecified role unspecified role prey prey purified purified F-ATPase beta subunit 4 predetermined predetermined participant predetermined predetermined predetermined participant predetermined unspecified role unspecified role prey prey purified purified his tag his tag his tag Hexa-His-tag 6-His-tag Histidine-tag Hexa-His-tag Histidine-tag 6-His-tag undetermined undetermined sequence position undetermined undetermined undetermined sequence position undetermined PEDF 6 predetermined predetermined participant predetermined predetermined predetermined participant predetermined unspecified role unspecified role bait bait purified purified physical association physical association homomint mint The F1 domain is composed of nine polypeptides with the stoichiometry α3β3γδε with a molecular weight of 370 kDa f2a; f2b; f3b plg-atp1 3 F-ATPase delta subunit 9 predetermined predetermined participant predetermined predetermined predetermined participant predetermined unspecified role unspecified role prey prey purified purified F-ATPase gamma subunit 7 predetermined predetermined participant predetermined predetermined predetermined participant predetermined unspecified role unspecified role prey prey purified purified F-ATPase beta subunit 4 predetermined predetermined participant predetermined predetermined predetermined participant predetermined unspecified role unspecified role prey prey purified purified his tag his tag his tag Hexa-His-tag 6-His-tag Histidine-tag Hexa-His-tag Histidine-tag 6-His-tag undetermined undetermined sequence position undetermined undetermined undetermined sequence position undetermined F-ATPase alpha subunit 8 predetermined predetermined participant predetermined predetermined predetermined participant predetermined unspecified role unspecified role prey prey purified purified F-ATPase epsilon subunit 10 predetermined predetermined participant predetermined predetermined predetermined participant predetermined unspecified role unspecified role prey prey purified purified angiostatin 5 predetermined predetermined participant predetermined predetermined predetermined participant predetermined unspecified role unspecified role bait bait purified purified binding site binding region binding-associated region binding region certain certain sequence position certain certain certain sequence position certain physical association physical association f2c homomint mint The F1 domain is composed of nine polypeptides with the stoichiometry α3β3γδε with a molecular weight of 370 kDa plg-atp1-1 1 F-ATPase delta subunit 9 predetermined predetermined participant predetermined predetermined predetermined participant predetermined unspecified role unspecified role prey prey purified purified F-ATPase epsilon subunit 10 predetermined predetermined participant predetermined predetermined predetermined participant predetermined unspecified role unspecified role prey prey purified purified F-ATPase gamma subunit 7 predetermined predetermined participant predetermined predetermined predetermined participant predetermined unspecified role unspecified role prey prey purified purified angiostatin 5 predetermined predetermined participant predetermined predetermined predetermined participant predetermined unspecified role unspecified role bait bait purified purified F-ATPase beta subunit 4 predetermined predetermined participant predetermined predetermined predetermined participant predetermined unspecified role unspecified role prey prey purified purified his tag his tag his tag Hexa-His-tag 6-His-tag Histidine-tag Hexa-His-tag Histidine-tag 6-His-tag undetermined undetermined sequence position undetermined undetermined undetermined sequence position undetermined F-ATPase alpha subunit 8 predetermined predetermined participant predetermined predetermined predetermined participant predetermined unspecified role unspecified role prey prey purified purified physical association physical association f3a homomint mint The F1 domain is composed of nine polypeptides with the stoichiometry α3β3γδε with a molecular weight of 370 kDa The SPR interactions between angiostatin and F1 were competed with PEDF.