UniProt UniProt http://www.uniprot.org enomoto-2006-6 in vitro In vitro atpase assay atpase assay predetermined predetermined participant predetermined Enomoto R., Kinebuchi T., Sato M., Yagi H., Kurumizaka H., Yokoyama S. kurumizaka@waseda.jp The Journal of biological chemistry 2006 Only protein-protein interactions imex curation imex curation enomoto-2006-2 ecoli Escherichia coli (strain K12) chromatography chromatography technology column chromatography chromatography weight by staining molecular weight estimation by staining weight by staining Enomoto R., Kinebuchi T., Sato M., Yagi H., Kurumizaka H., Yokoyama S. Proteins were coexpressed in ecoli with a N-terminal His-tag on PSMC3IP. The complex was purified by ammonium sulphare precpitation followed by Ni-NTA-agarose bead chromatography. The His tag was cleaved, and the complex purified by sequential Heparin-Sepharose chromatography and gel filtration (Superdex 200). kurumizaka@waseda.jp The Journal of biological chemistry 2006 Only protein-protein interactions imex curation imex curation enomoto-2006-3 ecoli Escherichia coli (strain K12) solution sedimentati cosedimentation in solution solution sedimentati predetermined predetermined participant predetermined Enomoto R., Kinebuchi T., Sato M., Yagi H., Kurumizaka H., Yokoyama S. kurumizaka@waseda.jp The Journal of biological chemistry 2006 Only protein-protein interactions imex curation imex curation enomoto-2006-4 ecoli Escherichia coli (strain K12) molecular sieving molecular sieving Gel Filtration Size Exclusion Chromatography Size Exclusion Chromatography Gel Filtration Sizing column predetermined predetermined participant predetermined Enomoto R., Kinebuchi T., Sato M., Yagi H., Kurumizaka H., Yokoyama S. kurumizaka@waseda.jp The Journal of biological chemistry 2006 Only protein-protein interactions imex curation imex curation dmc1_human Meiotic recombination protein DMC1/LIM15 homolog DMC1 DMC1H LIM15 protein protein human Homo sapiens Human MKEDQVVAEEPGFQDEEESLFQDIDLLQKHGINVADIKKLKSVGICTIKGIQMTTRRALCNVKGLSEAKVDKIKEAANKLIEPGFLTAFEYSEKRKMVFHITTGSQEFDKLLGGGIESMAITEAFGEFRTGKTQLSHTLCVTAQLPGAGGYPGGKIIFIDTENTFRPDRLRDIADRFNVDHDAVLDNVLYARAYTSEHQMELLDYVAAKFHEEAGIFKLLIIDSIMALFRVDFSGRGELAERQQKLAQMLSRLQKISEEYNVAVFVTNQMTADPGATMTFQADPKKPIGGHILAHASTTRISLRKGRGELRIAKIYDSPEMPENEATFAITAGGIGDAKE atp ATP Adenosine 5'-triphosphate Adenosine triphosphate ADENOSINE-5'-TRIPHOSPHATE Adephos Adetol Adynol Atipi ATP Atriphos Cardenosine Fosfobion Glucobasin H4atp Myotriphos Triadenyl Triphosphaden adenosine 5'-(tetrahydrogen triphosphate) small molecule small molecule chemical synthesis Chemical synthesis (Chemical synthesis) rad51_human DNA repair protein RAD51 homolog 1 RAD51 RAD51A RECA RAD51 homolog A protein protein human Homo sapiens Human MAMQMQLEANADTSVEEESFGPQPISRLEQCGINANDVKKLEEAGFHTVEAVAYAPKKELINIKGISEAKADKILAEAAKLVPMGFTTATEFHQRRSEIIQITTGSKELDKLLQGGIETGSITEMFGEFRTGKTQICHTLAVTCQLPIDRGGGEGKAMYIDTEGTFRPERLLAVAERYGLSGSDVLDNVAYARAFNTDHQTQLLYQASAMMVESRYALLIVDSATALYRTDYSGRGELSARQMHLARFLRMLLRLADEFGVAVVITNQVVAQVDGAAMFAADPKKPIGGNIIAHASTTRLYLRKGRGETRICKIYDSPCLPEAEAMFAINADGVGDAKD hop2_human Homologous-pairing protein 2 homolog PSMC3IP HOP2 Nuclear receptor coactivator GT198 PSMC3-interacting protein Proteasome 26S ATPase subunit 3-interacting protein TBPIP Tat-binding protein 1-interacting protein protein protein human Homo sapiens Human MSKGRAEAAAGAAGILLRYLQEQNRPYSSQDVFGNLQREHGLGKAVVVKTLEQLAQQGKIKEKMYGKQKIYFADQDQFDMVSDADLQVLDGKIVALTAKVQSLQQSCRYMEAELKELSSALTTPEMQKEIQELKKECAGYRERLKNIKAATNHVTPEEKEQVYRERQKYCKEWRKRKRMATELSDAILEGYPKSKKQFFEEVGIETDEDYNVTLPDP mnd1_human Meiotic nuclear division protein 1 homolog MND1 GAJ protein protein human Homo sapiens Human MSKKKGLSAEEKRTRMMEIFSETKDVFQLKDLEKIAPKEKGITAMSVKEVLQSLVDDGMVDCERIGTSNYYWAFPSKALHARKHKLEVLESQLSEGSQKHASLQKSIEKAKIGRCETEERTRLAKELSSLRDQREQLKAEVEKYKDCDPQVVEEIRQANKVAKEAANRWTDNIFAIKSWAKRKFGFEENKIDRTFGIPEDFDYID atp-dmc1-1 4054093 N/A 4054097 enzyme enzyme unspecified role unspecified role purified purified ecoli Escherichia coli (strain K12) N/A 4054098 enzyme target enzyme target substrate substrate unspecified role unspecified role region 32p radiolabel 32p radiolabel P32 32P 32P P32 undetermined undetermined sequence position undetermined undetermined undetermined sequence position undetermined false chemical synthesis Chemical synthesis (Chemical synthesis) atpase reaction atpase reaction false false false Fig.4 atp-rad51-1 4054093 N/A 4054099 enzyme enzyme unspecified role unspecified role purified purified ecoli Escherichia coli (strain K12) N/A 4054098 enzyme target enzyme target substrate substrate unspecified role unspecified role region 32p radiolabel 32p radiolabel P32 32P 32P P32 undetermined undetermined sequence position undetermined undetermined undetermined sequence position undetermined false chemical synthesis Chemical synthesis (Chemical synthesis) atpase reaction atpase reaction false false false Fig.4 mnd1-psmc3ip-1 4054094 N/A 4054100 unspecified role unspecified role neutral component neutral component purified purified N/A 4054101 unspecified role unspecified role neutral component neutral component purified purified direct interaction direct interaction false false false Fig. 1A mnd1-psmc3ip-2 4054095 N/A 4054100 unspecified role unspecified role neutral component neutral component purified purified Stoichiometry: 1.0 N/A 4054101 unspecified role unspecified role neutral component neutral component purified purified Stoichiometry: 1.0 direct interaction direct interaction false false false Fig. 1C mnd1-psmc3ip-3 4054096 N/A 4054100 unspecified role unspecified role neutral component neutral component purified purified Stoichiometry: 1.0 N/A 4054101 unspecified role unspecified role neutral component neutral component purified purified Stoichiometry: 1.0 direct interaction direct interaction false false false Fig. 1D