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 anonymous-2014h-1 Alt a 1 from Alternaria interacts with PR5 thaumatin-like proteins in vitro In vitro pull down pull down western blot western blot Immuno blot Immuno blot araceli.diaz@upm.es 2014 imex curation Gómez-Casado C., Murua-García A., Garrido-Arandia M., González-Melendi P., Sánchez-Monge R., Barber D., Pacios L.F., Díaz-Perales A. FEBS Lett. (0014-5793) Only protein-protein interactions anonymous-2014m-2 Alt a 1 from Alternaria interacts with PR5 thaumatin-like proteins in vitro In vitro pull down pull down ms participant Identification by mass spectrometry ms participant araceli.diaz@upm.es 2014 imex curation Gómez-Casado C., Murua-García A., Garrido-Arandia M., González-Melendi P., Sánchez-Monge R., Barber D., Pacios L.F., Díaz-Perales A. FEBS Lett. (0014-5793) Only protein-protein interactions tlp_actde Thaumatin-like protein tlp protein protein actde Actinidia deliciosa MSTFKSLSLSALLFIAFLFTCARGATFNIINNCPFTVWAAAVPGGGKRLDRGQNWIINPGAGTKGARVWPRTGCNFDGAGRGKCQTGDCNGLLQCQAFGQPPNTLAEYALNQFNNLDFFDISLVDGFNVAMEFSPTSGGCTRGIKCTADINGQCPNELRAPGGCNNPCTVFKTDQYCCNSGNCGLTNFSKFFKDRCPDAYSYPKDDQTSTFTCPAGTNYKVVFCP alta1_altal Major allergen Alt a 1 ALTA1 protein protein altal Alternaria alternata MQFTTIASLFAAAGLAAAAPLESRQDTASCPVTTEGDYVWKISEFYGRKPEGTYYNSLGFNIKATNGGTLDFTCSAQADKLEDHKWYSCGENSFMDFSFDSDRSGLLLKQKVSDDITYVATATLPNYCRAGGNGPKDFVCQGVADAYITLVTLPKSS b6cqt3_9rosa Pru p 2.02 protein protein prunus dulcis x prunus persica Prunus dulcis x Prunus persica MMKTLVAVLSLSLTLLSFGGAHAATMSFKNNCPYTVWPASFGNPQLSTTGFELASQASFQLDTPVPWSGRFWARTRCSTDASGKFVCETADCDSGQLMCNGKTGIPPATLAEFTIAAGGGQDFYDVSLVDGFNLPMSVTPQGGTGTCKMGSCAANVNLVCPSELQKIGSDGSVVACLSACVKFGEPQYCCTPPQETKEKCPPTNYSQIFHEQCPDAYSYAFDDNKGLFTCSGGPNYLITFCP i3rtu5_musac Thau protein protein musac Musa acuminata MVSSTILSFLLFALLLALSRAVTFEIVNGCPFTVWPAAVPGGGLQLDQGQTWVLDVNPGTTGGRIWARTGCSFDGSGSGSCQTGDCGGVLDCKGYGSPPNTVAEFAVGQFNNFDVSLVDGFNVPMEFGSCRAIRCSADINGRCPAELRTPGGCNNPCTVFKTDEYCCTSGSCGPTTYSKFFKSNCPDAYSYPKDDATSTFTCPGNGDYKVIFCPSVSSLPADGYPTRFGRIAVSFVIPKASGT alta1-tlp-2 1499595 n/a PR5-thaumatin- like protein 1499597 western blot western blot Immuno blot Immuno blot unspecified role unspecified role prey prey purified purified n/a Alt a 1 1499598 western blot western blot Immuno blot Immuno blot unspecified role unspecified role bait bait purified purified direct interaction direct interaction false false false f2a Pull down assays were carried out to find potential plant receptors for Alt a 1. Dynabeads® M-280 Tosylactivated (Invitrogen, Oslo, Norway) were coated with Alt a 1 (Bial 172 Aristegui, Bilbao Spain) and incubated with a kiwifruit protein extract (Figure 2A). A principal band around 26 kDa was observed when the immunoprecipitated proteins were separated by SDS-PAGE and stained with Coomassie. This band was identified by mass fingerprinting as the 175 PR5-thaumatin like protein (P81370). The accuracy of the retained protein identification was further supported by immunodetection using specific polyclonal antibodies against PR5 (Anti- PR5). alta1-tlp-3 1499595 n/a peach PR5 1499599 western blot western blot Immuno blot Immuno blot unspecified role unspecified role prey prey purified purified n/a Alt a 1 1499598 western blot western blot Immuno blot Immuno blot unspecified role unspecified role bait bait purified purified direct interaction direct interaction false false false f2a Pull down assays were carried out to find potential plant receptors for Alt a 1. Dynabeads® M-280 Tosylactivated (Invitrogen, Oslo, Norway) were coated with Alt a 1 (Bial 172 Aristegui, Bilbao Spain) and incubated with a kiwifruit protein extract (Figure 2A). A principal band around 26 kDa was observed when the immunoprecipitated proteins were separated by SDS-PAGE and stained with Coomassie. This band was identified by mass fingerprinting as the 175 PR5-thaumatin like protein (P81370). The accuracy of the retained protein identification was further supported by immunodetection using specific polyclonal antibodies against PR5 (Anti- PR5). alta1-pru_p_2_02 1499595 n/a banana PR5 1499600 western blot western blot Immuno blot Immuno blot unspecified role unspecified role prey prey purified purified n/a Alt a 1 1499598 western blot western blot Immuno blot Immuno blot unspecified role unspecified role bait bait purified purified direct interaction direct interaction false false false f2a Pull down assays were carried out to find potential plant receptors for Alt a 1. Dynabeads® M-280 Tosylactivated (Invitrogen, Oslo, Norway) were coated with Alt a 1 (Bial 172 Aristegui, Bilbao Spain) and incubated with a kiwifruit protein extract (Figure 2A). A principal band around 26 kDa was observed when the immunoprecipitated proteins were separated by SDS-PAGE and stained with Coomassie. This band was identified by mass fingerprinting as the 175 PR5-thaumatin like protein (P81370). The accuracy of the retained protein identification was further supported by immunodetection using specific polyclonal antibodies against PR5 (Anti- PR5). tlp-alta1 1499595 n/a Alt a 1 1499598 ms participant Identification by mass spectrometry ms participant unspecified role unspecified role prey prey purified purified n/a PR5-thaumatin- like protein 1499597 western blot western blot Immuno blot Immuno blot unspecified role unspecified role bait bait purified purified direct interaction direct interaction false false false f2b Pull down assays were carried out to find potential plant receptors for Alt a 1. Dynabeads® M-280 Tosylactivated (Invitrogen, Oslo, Norway) were coated with Alt a 1 (Bial 172 Aristegui, Bilbao Spain) and incubated with a kiwifruit protein extract (Figure 2A). A principal band around 26 kDa was observed when the immunoprecipitated proteins were separated by SDS-PAGE and stained with Coomassie. This band was identified by mass fingerprinting as the 175 PR5-thaumatin like protein (P81370). The accuracy of the retained protein identification was further supported by immunodetection using specific polyclonal antibodies against PR5 (Anti- PR5). alta1-tlp-1 1499596 n/a Alt a 1 1499598 predetermined predetermined participant predetermined unspecified role unspecified role bait bait purified purified n/a PR5-thaumatin- like protein 1499597 ms participant Identification by mass spectrometry ms participant unspecified role unspecified role prey prey cell lysate cell lysate physical association physical association false false false f2a Pull down assays were carried out to find potential plant receptors for Alt a 1. Dynabeads® M-280 Tosylactivated (Invitrogen, Oslo, Norway) were coated with Alt a 1 (Bial 172 Aristegui, Bilbao Spain) and incubated with a kiwifruit protein extract (Figure 2A). A principal band around 26 kDa was observed when the immunoprecipitated proteins were separated by SDS-PAGE and stained with Coomassie. This band was identified by mass fingerprinting as the 175 PR5-thaumatin like protein (P81370). The accuracy of the retained protein identification was further supported by immunodetection using specific polyclonal antibodies against PR5 (Anti- PR5).