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 The phosphatase Ppt1 is a dedicated regulator of the molecular chaperone Hsp90. The phosphatase Ppt1 is a dedicated regulator of the molecular chaperone Hsp90. EMBO J. (0261-4189) 2006 imex curation Wandinger SK., Suhre MH., Wegele H., Buchner J. 2009-01-08 Only protein-protein interactions in vitro In vitro elisa enzyme linked immunosorbent assay ELISA ELISA elisa nucleotide sequence nucleotide sequence identification sequence cloning sequence cloning nucleotide sequence Wandinger SK., Suhre MH., Wegele H., Buchner J. EMBO J. (0261-4189) 2006 2009-01-08 Only protein-protein interactions imex curation The phosphatase Ppt1 is a dedicated regulator of the molecular chaperone Hsp90. The phosphatase Ppt1 is a dedicated regulator of the molecular chaperone Hsp90. EMBO J. (0261-4189) 2006 imex curation Wandinger SK., Suhre MH., Wegele H., Buchner J. 2009-01-08 Only protein-protein interactions in vitro In vitro itc isothermal titration calorimetry ITC ITC itc nucleotide sequence nucleotide sequence identification sequence cloning sequence cloning nucleotide sequence Wandinger SK., Suhre MH., Wegele H., Buchner J. EMBO J. (0261-4189) 2006 2009-01-08 Only protein-protein interactions imex curation The phosphatase Ppt1 is a dedicated regulator of the molecular chaperone Hsp90. The phosphatase Ppt1 is a dedicated regulator of the molecular chaperone Hsp90. EMBO J. (0261-4189) 2006 imex curation Wandinger SK., Suhre MH., Wegele H., Buchner J. 2009-01-08 Only protein-protein interactions in vitro In vitro enzymatic study enzymatic study nucleotide sequence nucleotide sequence identification sequence cloning sequence cloning nucleotide sequence Wandinger SK., Suhre MH., Wegele H., Buchner J. EMBO J. (0261-4189) 2006 2009-01-08 Only protein-protein interactions imex curation sti1_yeast Heat shock protein STI1 STI1 OR26.17 YOR027W protein protein yeast Saccharomyces cerevisiae Baker's yeast MSLTADEYKQQGNAAFTAKDYDKAIELFTKAIEVSETPNHVLYSNRSACYTSLKKFSDALNDANECVKINPSWSKGYNRLGAAHLGLGDLDEAESNYKKALELDASNKAAKEGLDQVHRTQQARQAQPDLGLTQLFADPNLIENLKKNPKTSEMMKDPQLVAKLIGYKQNPQAIGQDLFTDPRLMTIMATLMGVDLNMDDINQSNSMPKEPETSKSTEQKKDAEPQSDSTTSKENSSKAPQKEESKESEPMEVDEDDSKIEADKEKAEGNKFYKARQFDEAIEHYNKAWELHKDITYLNNRAAAEYEKGEYETAISTLNDAVEQGREMRADYKVISKSFARIGNAYHKLGDLKKTIEYYQKSLTEHRTADILTKLRNAEKELKKAEAEAYVNPEKAEEARLEGKEYFTKSDWPNAVKAYTEMIKRAPEDARGYSNRAAALAKLMSFPEAIADCNKAIEKDPNFVRAYIRKATAQIAVKEYASALETLDAARTKDAEVNNGSSAREIDQLYYKASQQRFQPGTSNETPEETYQRAMKDPEVAAIMQDPVMQSILQQAQQNPAALQEHMKNPEVFKKIQTLIAAGIIRTGR CF8A85C2BBD3C44C CF8A85C2BBD3C44C ppt1_yeast Serine/threonine-protein phosphatase T PPT1 G6347 YGR123C protein protein yeast Saccharomyces cerevisiae Baker's yeast MSTPTAADRAKALERKNEGNVFVKEKHFLKAIEKYTEAIDLDSTQSIYFSNRAFAHFKVDNFQSALNDCDEAIKLDPKNIKAYHRRALSCMALLEFKKARKDLNVLLKAKPNDPAATKALLTCDRFIREERFRKAIGGAENEAKISLCQTLNLSSFDANADLANYEGPKLEFEQLYDDKNAFKGAKIKNMSQEFISKMVNDLFLKGKYLPKKYVAAIISHADTLFRQEPSMVELENNSTPDVKISVCGDTHGQFYDVLNLFRKFGKVGPKHTYLFNGDFVDRGSWSCEVALLFYCLKILHPNNFFLNRGNHESDNMNKIYGFEDECKYKYSQRIFNMFAQSFESLPLATLINNDYLVMHGGLPSDPSATLSDFKNIDRFAQPPRDGAFMELLWADPQEANGMGPSQRGLGHAFGPDITDRFLRNNKLRKIFRSHELRMGGVQFEQKGKLMTVFSAPNYCDSQGNLGGVIHVVPGHGILQAGRNDDQNLIIETFEAVEHPDIKPMAYSNGGFGL 6966DA22340A5793 6966DA22340A5793 hsp82_yeast ATP-dependent molecular chaperone HSP82 HSP90 YPL240C HSP82 Heat shock protein Hsp90 heat-inducible isoform 82 kDa heat shock protein protein protein yeast Saccharomyces cerevisiae Baker's yeast MASETFEFQAEITQLMSLIINTVYSNKEIFLRELISNASDALDKIRYKSLSDPKQLETEPDLFIRITPKPEQKVLEIRDSGIGMTKAELINNLGTIAKSGTKAFMEALSAGADVSMIGQFGVGFYSLFLVADRVQVISKSNDDEQYIWESNAGGSFTVTLDEVNERIGRGTILRLFLKDDQLEYLEEKRIKEVIKRHSEFVAYPIQLVVTKEVEKEVPIPEEEKKDEEKKDEEKKDEDDKKPKLEEVDEEEEKKPKTKKVKEEVQEIEELNKTKPLWTRNPSDITQEEYNAFYKSISNDWEDPLYVKHFSVEGQLEFRAILFIPKRAPFDLFESKKKKNNIKLYVRRVFITDEAEDLIPEWLSFVKGVVDSEDLPLNLSREMLQQNKIMKVIRKNIVKKLIEAFNEIAEDSEQFEKFYSAFSKNIKLGVHEDTQNRAALAKLLRYNSTKSVDELTSLTDYVTRMPEHQKNIYYITGESLKAVEKSPFLDALKAKNFEVLFLTDPIDEYAFTQLKEFEGKTLVDITKDFELEETDEEKAEREKEIKEYEPLTKALKEILGDQVEKVVVSYKLLDAPAAIRTGQFGWSANMERIMKAQALRDSSMSSYMSSKKTFEISPKSPIIKELKKRVDEGGAQDKTVKDLTKLLYETALLTSGFSLDEPTSFASRINRLISLGLNIDEDEETETAPEASTAAPVEEVPADTEMEEVD D7C35676D668FB63 D7C35676D668FB63 ppt1-hsp82-3 1 6 nucleotide sequence nucleotide sequence identification sequence cloning sequence cloning nucleotide sequence predetermined predetermined participant predetermined unspecified role unspecified role prey prey 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 Dimerization domain range MINT-2516981: original sequence: 530-709 : LEETDEEKAEREKEIKEYEPLTKALKEILGDQVEKVVVSYKLLDAPAAIRTGQFGWSANMERIMKAQALRDSSMSSYMSSKKTFEISPKSPIIKELKKRVDEGGAQDKTVKDLTKLLYETALLTSGFSLDEPTSFASRINRLISLGLNIDEDEETETAPEASTAAPVEEVPADTEMEEV Stoichiometry: 1.0 5 nucleotide sequence nucleotide sequence identification sequence cloning sequence cloning nucleotide sequence predetermined predetermined participant predetermined 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 range MINT-2516968: original sequence: 1-170 : MSTPTAADRAKALERKNEGNVFVKEKHFLKAIEKYTEAIDLDSTQSIYFSNRAFAHFKVDNFQSALNDCDEAIKLDPKNIKAYHRRALSCMALLEFKKARKDLNVLLKAKPNDPAATKALLTCDRFIREERFRKAIGGAENEAKISLCQTLNLSSFDANADLANYEGPK Stoichiometry: 1.0 direct interaction direct interaction F1C EMBO-Journal fragments of Ppt1 were generated (Figure 1B) and used in a modified ELISA to determine the association of Ppt1 and Ppt1 fragments with yHsp90 mint sti1-hsp82-11 1 6 nucleotide sequence nucleotide sequence identification sequence cloning sequence cloning nucleotide sequence predetermined predetermined participant predetermined unspecified role unspecified role prey prey 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 Dimerization domain range MINT-2516987: original sequence: 530-709 : LEETDEEKAEREKEIKEYEPLTKALKEILGDQVEKVVVSYKLLDAPAAIRTGQFGWSANMERIMKAQALRDSSMSSYMSSKKTFEISPKSPIIKELKKRVDEGGAQDKTVKDLTKLLYETALLTSGFSLDEPTSFASRINRLISLGLNIDEDEETETAPEASTAAPVEEVPADTEMEEV Stoichiometry: 1.0 4 nucleotide sequence nucleotide sequence identification sequence cloning sequence cloning nucleotide sequence predetermined predetermined participant predetermined unspecified role unspecified role bait bait purified purified Stoichiometry: 1.0 direct interaction direct interaction F1C EMBO-Journal mint hsp82-ppt1-3 2 5 nucleotide sequence nucleotide sequence identification sequence cloning sequence cloning nucleotide sequence predetermined predetermined participant predetermined unspecified role unspecified role neutral component neutral component purified purified Stoichiometry: 1.0 6 nucleotide sequence nucleotide sequence identification sequence cloning sequence cloning nucleotide sequence predetermined predetermined participant predetermined unspecified role unspecified role neutral component neutral component purified purified Stoichiometry: 1.0 direct interaction direct interaction F1A EMBO-Journal the ITC data show that two Ppt1 molecules bind to a yHsp90 dimer. kd 670 nanomolar mint hsp82-ppt1-4 3 5 nucleotide sequence nucleotide sequence identification sequence cloning sequence cloning nucleotide sequence predetermined predetermined participant predetermined enzyme enzyme neutral component neutral component purified purified Stoichiometry: 1.0 6 nucleotide sequence nucleotide sequence identification sequence cloning sequence cloning nucleotide sequence predetermined predetermined participant predetermined enzyme target enzyme target substrate substrate neutral component neutral component purified purified undefined mutation mutation disrupting interaction mutation disrupting mutation disrupting interaction mutation disrupting deletion analysis deletion analysis certain certain sequence position certain certain certain sequence position certain Wed Jul 06 15:01:06 BST 2016 Sequence change details about this feature cannot be ascertained or do not fit with the current version of the referenced protein, so they have been deleted as a result of our quality control procedures. The original label was mutation disrupting 705-709 range MINT-2779182: original sequence: 705-709 : PVEEVPADTEMEEV binding site binding region binding-associated region binding region certain certain sequence position certain certain certain sequence position certain Dimerization domain range MINT-2779186: original sequence: 530-709 : LEETDEEKAEREKEIKEYEPLTKALKEILGDQVEKVVVSYKLLDAPAAIRTGQFGWSANMERIMKAQALRDSSMSSYMSSKKTFEISPKSPIIKELKKRVDEGGAQDKTVKDLTKLLYETALLTSGFSLDEPTSFASRINRLISLGLNIDEDEETETAPEASTAAPVEEVPADTEMEEV Stoichiometry: 1.0 dephosphorylation dephosphorylation reaction dephosphorylation F3A F4A EMBO-Journal Ppt1 specifically dephosphorylates Hsp90 mint