IntAct European Bioinformatics Institute IntAct intact http://www.ebi.ac.uk/ http://www.ebi.ac.uk/intact/query/${ac} EBI-[0-9]+|IA:[0-9]+ INTerAction database (IntAct) provides an open source database and toolkit for the storage, presentation and analysis of molecular interactions. http://www.ebi.ac.uk/intact European Bioinformatics Institute; Wellcome Trust Genome Campus; Hinxton, Cambridge; CB10 1SD; United Kingdom http://www.ebi.ac.uk/intact/ http://www.ebi.ac.uk/ zhu-2004-1 Crystal structure of human GGA1 GAT domain complexed with the GAT-binding domain of Rabaptin5. in vitro In vitro x-ray diffraction x-ray crystallography X-ray X-ray x-ray diffraction predetermined predetermined participant predetermined Zhu G., Zhai P., He X., Wakeham N., Rodgers K., Li G., Tang J., Zhang XC. Synapse - Interactions of proteins with an established role in the presynapse. EMBO J. (0261-4189) 2004 Apoptosis - Interactions involving proteins with a function related to apoptosis zhu-2004-2 Crystal structure of human GGA1 GAT domain complexed with the GAT-binding domain of Rabaptin5. in vitro In vitro pull down pull down western blot western blot Immuno blot Immuno blot Zhu G., Zhai P., He X., Wakeham N., Rodgers K., Li G., Tang J., Zhang XC. Synapse - Interactions of proteins with an established role in the presynapse. EMBO J. (0261-4189) 2004 Apoptosis - Interactions involving proteins with a function related to apoptosis zhu-2004-3 Crystal structure of human GGA1 GAT domain complexed with the GAT-binding domain of Rabaptin5. in vitro In vitro crosslink cross-linking study crosslink western blot western blot Immuno blot Immuno blot Zhu G., Zhai P., He X., Wakeham N., Rodgers K., Li G., Tang J., Zhang XC. Synapse - Interactions of proteins with an established role in the presynapse. EMBO J. (0261-4189) 2004 Apoptosis - Interactions involving proteins with a function related to apoptosis gga1_human ADP-ribosylation factor-binding protein GGA1 Golgi-localized, gamma ear-containing, ARF-binding protein 1 Gamma-adaptin-related protein 1 GGA1 protein protein human Homo sapiens Human MEPAMEPETLEARINRATNPLNKELDWASINGFCEQLNEDFEGPPLATRLLAHKIQSPQEWEAIQALTVLETCMKSCGKRFHDEVGKFRFLNELIKVVSPKYLGSRTSEKVKNKILELLYSWTVGLPEEVKIAEAYQMLKKQGIVKSDPKLPDDTTFPLPPPRPKNVIFEDEEKSKMLARLLKSSHPEDLRAANKLIKEMVQEDQKRMEKISKRVNAIEEVNNNVKLLTEMVMSHSQGGAAAGSSEDLMKELYQRCERMRPTLFRLASDTEDNDEALAEILQANDNLTQVINLYKQLVRGEEVNGDATAGSIPGSTSALLDLSGLDLPPAGTTYPAMPTRPGEQASPEQPSASVSLLDDELMSLGLSDPTPPSGPSLDGTGWNSFQSSDATEPPAPALAQAPSMESRPPAQTSLPASSGLDDLDLLGKTLLQQSLPPESQQVRWEKQQPTPRLTLRDLQNKSSSCSSPSSSATSLLHTVSPEPPRPPQQPVPTELSLASITVPLESIKPSNILPVTVYDQHGFRILFHFARDPLPGRSDVLVVVVSMLSTAPQPIRNIVFQSAVPKVMKVKLQPPSGTELPAFNPIVHPSAITQVLLLANPQKEKVRLRYKLTFTMGDQTYNEMGDVDQFPPPETWGSL rabe1_human Rab GTPase-binding effector protein 1 Rabaptin-5 Rabaptin-5alpha Rabaptin-4 Renal carcinoma antigen NY-REN-17 RABEP1 RABPT5 RABPT5A RAB5EP protein protein human Homo sapiens Human MAQPGPASQPDVSLQQRVAELEKINAEFLRAQQQLEQEFNQKRAKFKELYLAKEEDLKRQNAVLQAAQDDLGHLRTQLWEAQAEMENIKAIATVSENTKQEAIDEVKRQWREEVASLQAVMKETVRDYEHQFHLRLEQERTQWAQYRESAEREIADLRRRLSEGQEEENLENEMKKAQEDAEKLRSVVMPMEKEIAALKDKLTEAEDKIKELEASKVKELNHYLEAEKSCRTDLEMYVAVLNTQKSVLQEDAEKLRKELHEVCHLLEQERQQHNQLKHTWQKANDQFLESQRLLMRDMQRMEIVLTSEQLRQVEELKKKDQEDDEQQRLNKRKDHKKADVEEEIKIPVVCALTQEESSAQLSNEEEHLDSTRGSVHSLDAGLLLPSGDPFSKSDNDMFKDGLRRAQSTDSLGTSGSLQSKALGYNYKAKSAGNLDESDFGPLVGADSVSENFDTASLGSLQMPSGFMLTKDQERAIKAMTPEQEETASLLSSVTQGMESAYVSPSGYRLVSETEWNLLQKEVHNAGNKLGRRCDMCSNYEKQLQGIQIQEAETRDQVKKLQLMLRQANDQLEKTMKDKQELEDFIKQSSEDSSHQISALVLRAQASEILLEELQQGLSQAKRDVQEQMAVLMQSREQVSEELVRLQKDNDSLQGKHSLHVSLQQAEDFILPDTTEALRELVLKYREDIINVRTAADHVEEKLKAEILFLKEQIQAEQCLKENLEETLQLEIENCKEEIASISSLKAELERIKVEKGQLESTLREKSQQLESLQEIKISLEEQLKKETAAKATVEQLMFEEKNKAQRLQTELDVSEQVQRDFVKLSQTLQVQLERIRQADSLERIRAILNDTKLTDINQLPET gga1-rabep1-1 crystal structure of human GGA1 GAT domain and GAT-binding domain of human Rabaptin-5 145792 N/A 145795 unspecified role unspecified role neutral component neutral component gat domain binding region binding-associated region binding region certain certain sequence position certain certain certain sequence position certain false ecobb Escherichia coli (strain B / BL21) Stoichiometry: 1.0 N/A 145796 unspecified role unspecified role neutral component neutral component gat binding binding region binding-associated region binding region certain certain sequence position certain certain certain sequence position certain false ecobb Escherichia coli (strain B / BL21) Stoichiometry: 2.0 direct interaction direct interaction false false false 2.41 working 23.3%, free 28.3% gga1-rabep1-2 GST pull-down ,bait= human GAA1 GAT domain, prey= rabaptin-5 full-length and 551-661 fragment 145793 N/A 145796 unspecified role unspecified role prey prey Q15276:p.Gln566Ala mutation decreasing mutation decreasing interaction hotspot hotspot mutation decreasing certain certain sequence position certain certain certain sequence position certain false Q15276:p.Gln566Arg mutation decreasing mutation decreasing interaction hotspot hotspot mutation decreasing certain certain sequence position certain certain certain sequence position certain false Q15276:p.Asn568Arg mutation decreasing mutation decreasing interaction hotspot hotspot mutation decreasing certain certain sequence position certain certain certain sequence position certain false gat binding binding region binding-associated region binding region certain certain sequence position certain certain certain sequence position certain false Q15276:p.Gln561Ala mutation decreasing mutation decreasing interaction hotspot hotspot mutation decreasing certain certain sequence position certain certain certain sequence position certain false Q15276:p.Met563Arg mutation decreasing mutation decreasing interaction hotspot hotspot mutation decreasing certain certain sequence position certain certain certain sequence position certain false human-293 Homo sapiens transformed primary embryonal kidney cells Human 293 Transformed human primary embryonal kidney cells. The Cell type named 293 is synonymous with HEK-293. N/A 145795 unspecified role unspecified role bait bait gat domain binding region binding-associated region binding region certain certain sequence position certain certain certain sequence position certain false region gst tag glutathione s tranferase tag glutathione S-tranferase tag glutathione S-tranferase tag gst tag undetermined undetermined sequence position undetermined undetermined undetermined sequence position undetermined false ecobb Escherichia coli (strain B / BL21) physical association physical association false false false GAT-binding domain of Rabaptin-5 (551-661) produced in E. coli competes with Rabaptin full-length for binding to GST-GAT domain of GAA1 rabep1-rabep1-1 cross-linking of rabaptin-5 551-661 fragments 145794 N/A 145796 unspecified role unspecified role neutral component neutral component region binding region binding-associated region binding region certain certain sequence position certain certain certain sequence position certain false region 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 false ecobb Escherichia coli (strain B / BL21) Stoichiometry: 1.0 N/A 145796 unspecified role unspecified role neutral component neutral component region binding region binding-associated region binding region certain certain sequence position certain certain certain sequence position certain false region 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 false ecobb Escherichia coli (strain B / BL21) Stoichiometry: 2.0 physical association physical association false false false A significant fraction of Rabaptin-5 forms dimers, trimers and tetramers. Double mutant (L610R/L613W) of Rabaptin-5 fragment (551-661) cannot form oligomer with a MW higher than a dimer.