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/ Crystal structure of human GGA1 GAT domain complexed with the GAT-binding domain of Rabaptin5. Crystal structure of human GGA1 GAT domain complexed with the GAT-binding domain of Rabaptin5. EMBO J. (0261-4189) 2004 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. Apoptosis - Interactions involving proteins with a function related to apoptosis 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. Accepted 2010-JAN-10 by SKERRIEN (applied to all records created before 2005-Sep-01). EMBO J. (0261-4189) 2004 Crystal structure of human GGA1 GAT domain complexed with the GAT-binding domain of Rabaptin5. Crystal structure of human GGA1 GAT domain complexed with the GAT-binding domain of Rabaptin5. EMBO J. (0261-4189) 2004 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. Apoptosis - Interactions involving proteins with a function related to apoptosis 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. Accepted 2010-JAN-10 by SKERRIEN (applied to all records created before 2005-Sep-01). EMBO J. (0261-4189) 2004 Crystal structure of human GGA1 GAT domain complexed with the GAT-binding domain of Rabaptin5. Crystal structure of human GGA1 GAT domain complexed with the GAT-binding domain of Rabaptin5. EMBO J. (0261-4189) 2004 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. Apoptosis - Interactions involving proteins with a function related to apoptosis 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. Accepted 2010-JAN-10 by SKERRIEN (applied to all records created before 2005-Sep-01). EMBO J. (0261-4189) 2004 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 B0B6F089FA0F7DD5 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 DIP protein Q15276 original sequence version: 59 CAAF91638B8ED516 gga1-rabep1-1 2 4 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 ecobb Escherichia coli (strain B / BL21) 5 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 ecobb Escherichia coli (strain B / BL21) direct interaction direct interaction 2.41 working 23.3%, free 28.3% gga1-rabep1-2 3 5 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 Q A Wed May 02 19:53:35 BST 2018 This feature has been corrected as a result of our quality control procedures. The original label was 'gln566ala' Tue Jun 30 18:43:18 BST 2020 This feature has been corrected as a result of our quality control procedures. The original label was 'p.Gln566Ala' Q15276:p.Gln566Arg mutation decreasing mutation decreasing interaction hotspot hotspot mutation decreasing certain certain sequence position certain certain certain sequence position certain Q R Wed May 02 14:47:33 BST 2018 This feature has been corrected as a result of our quality control procedures. The original label was 'gln566arg' Tue Jun 30 20:04:15 BST 2020 This feature has been corrected as a result of our quality control procedures. The original label was 'p.Gln566Arg' Q15276:p.Asn568Arg mutation decreasing mutation decreasing interaction hotspot hotspot mutation decreasing certain certain sequence position certain certain certain sequence position certain N R Wed May 02 16:47:48 BST 2018 This feature has been corrected as a result of our quality control procedures. The original label was 'asn568arg' Tue Jun 30 15:57:15 BST 2020 This feature has been corrected as a result of our quality control procedures. The original label was 'p.Asn568Arg' gat binding binding region binding-associated region binding region certain certain sequence position certain certain certain sequence position certain Q15276:p.Gln561Ala mutation decreasing mutation decreasing interaction hotspot hotspot mutation decreasing certain certain sequence position certain certain certain sequence position certain Q A Wed May 02 15:49:42 BST 2018 This feature has been corrected as a result of our quality control procedures. The original label was 'gln561ala' Tue Jun 30 19:56:14 BST 2020 This feature has been corrected as a result of our quality control procedures. The original label was 'p.Gln561Ala' Q15276:p.Met563Arg mutation decreasing mutation decreasing interaction hotspot hotspot mutation decreasing certain certain sequence position certain certain certain sequence position certain M R Wed May 02 14:28:14 BST 2018 This feature has been corrected as a result of our quality control procedures. The original label was 'met563arg' Tue Jun 30 16:59:57 BST 2020 This feature has been corrected as a result of our quality control procedures. The original label was 'p.Met563Arg' 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. 4 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 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 ecobb Escherichia coli (strain B / BL21) physical association physical association 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 1 5 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 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 ecobb Escherichia coli (strain B / BL21) 5 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 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 ecobb Escherichia coli (strain B / BL21) physical association physical association 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.