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/ Serine 331 and tyrosine 333 are both involved in the interaction between the cytosolic domain of TGN38 and the mu2 subunit of the AP2 clathrin adaptor complex. Serine 331 and tyrosine 333 are both involved in the interaction between the cytosolic domain of TGN38 and the mu2 subunit of the AP2 clathrin adaptor complex. J. Biol. Chem. (0021-9258) 1997 Stephens DJ., Crump CM., Clarke AR., Banting G. in vitro In vitro anti tag coip anti tag coimmunoprecipitation anti tag coip predetermined predetermined participant predetermined Stephens DJ., Crump CM., Clarke AR., Banting G. interacting proteins were detected by measuring bands intensity after SDS-PAGE staining. J. Biol. Chem. (0021-9258) 1997 Serine 331 and tyrosine 333 are both involved in the interaction between the cytosolic domain of TGN38 and the mu2 subunit of the AP2 clathrin adaptor complex. Serine 331 and tyrosine 333 are both involved in the interaction between the cytosolic domain of TGN38 and the mu2 subunit of the AP2 clathrin adaptor complex. J. Biol. Chem. (0021-9258) 1997 Stephens DJ., Crump CM., Clarke AR., Banting G. in vitro In vitro fluorescence spectr classical fluorescence spectroscopy fluorescence spectr predetermined predetermined participant predetermined Stephens DJ., Crump CM., Clarke AR., Banting G. J. Biol. Chem. (0021-9258) 1997 Serine 331 and tyrosine 333 are both involved in the interaction between the cytosolic domain of TGN38 and the mu2 subunit of the AP2 clathrin adaptor complex. Serine 331 and tyrosine 333 are both involved in the interaction between the cytosolic domain of TGN38 and the mu2 subunit of the AP2 clathrin adaptor complex. J. Biol. Chem. (0021-9258) 1997 Stephens DJ., Crump CM., Clarke AR., Banting G. yeasx Saccharomyces cerevisiae (Baker's yeast) Baker's yeast 2 hybrid two hybrid 2H 2h Gal4 transcription regeneration two-hybrid yeast two hybrid 2-hybrid classical two hybrid classical two hybrid 2H two-hybrid 2-hybrid Gal4 transcription regeneration 2h yeast two hybrid Y2H Y-2H 2 hybrid predetermined predetermined participant predetermined Stephens DJ., Crump CM., Clarke AR., Banting G. J. Biol. Chem. (0021-9258) 1997 ap2m1_rat AP-2 complex subunit mu Adaptor protein complex AP-2 subunit mu AP-2 mu chain Ap2m1 Mu2-adaptin Plasma membrane adaptor AP-2 50 kDa protein Clathrin coat assembly protein AP50 Clathrin coat-associated protein AP50 Clathrin assembly protein complex 2 mu medium chain Adaptor-related protein complex 2 subunit mu protein protein rat Rattus norvegicus (Rat) Rat MIGGLFIYNHKGEVLISRVYRDDIGRNAVDAFRVNVIHARQQVRSPVTNIARTSFFHVKRSNIWLAAVTKQNVNAAMVFEFLYKMCDVMAAYFGKISEENIKNNFVLIYELLDEILDFGYPQNSETGALKTFITQQGIKSQHQTKEEQSQITSQVTGQIGWRREGIKYRRNELFLDVLESVNLLMSPQGQVLSAHVSGRVVMKSYLSGMPECKFGMNDKIVIEKQGKGTADETSKSGKQSIAIDDCTFHQCVRLSKFDSERSISFIPPDGEFELMRYRTTKDIILPFRVIPLVREVGRTKLEVKVVIKSNFKPSLLAQKIEVRIPTPLNTSGVQVICMKGKAKYKASENAIVWKIKRMAGMKESQISAEIELLPTNDKKKWARPPISMNFEVPFAPSGLKVRYLKVFEPKLNYSDHDVIKWVRYIGRSGIYETRC DIP protein P84092 original sequence version: 91 DIP protein P84092 original sequence version: 42 DIP protein P84092 original sequence version: 82 DIP protein P84092 original sequence version: 67 DIP protein P84092 original sequence version: 92 DIP protein P84092 original sequence version: 105 DIP protein P84092 original sequence version: 110 82803219BA279954 tgon3_rat Trans-Golgi network integral membrane protein TGN38 Ttgn1 protein protein rat Rattus norvegicus (Rat) Rat MQFLVALLLLSVAVARALPSASKPNNTSSENNPPIQPSTPLPPGVDISQQVKTNRPTDQRLESDKEGQDKTVARTSASVSSGVESATNLNLDDSKKHPETADAKLKETLQQLLPVDPKQEKSGQKFTKDSGSPTGGDSDNTTGGDSNKTTGVDSDKTSGGDSNKPTGSDNDKPTGGDSNKPTSKVPSNTETPKIDKVQLTEKGQKPTLISKTESGEKLAGDSDFSLKPEKGDKSSEPTEDVETKEIEEGDTEPEEGSPLEEENEKVLGPSSSENQEGTLTDSMKDEKDDHYKDNSGNTSAESSHFFAYLVTAAVLVAVLYIAYHNKRKIIAFALEGKRSKVTRRPKASDYQRLNLKL 173B64C51CAD593B ap2m1-tgn41-3 3 4 unspecified role unspecified role prey prey 5 unspecified role unspecified role bait bait P19814:p.Tyr350Ala mutation decreasing mutation decreasing interaction hotspot hotspot mutation decreasing certain certain sequence position certain certain certain sequence position certain Y A Wed May 02 18:52:48 BST 2018 This feature has been corrected as a result of our quality control procedures. The original label was 'tyr350ala' Tue Jun 30 19:04:18 BST 2020 This feature has been corrected as a result of our quality control procedures. The original label was 'p.Tyr350Ala' cytoplasmic domain binding region binding-associated region binding region certain certain sequence position certain certain certain sequence position certain P19814:p.Ser348Ala mutation decreasing mutation decreasing interaction hotspot hotspot mutation decreasing mutation analysis mutation analysis certain certain sequence position certain certain certain sequence position certain S A Wed May 02 18:43:06 BST 2018 This feature has been corrected as a result of our quality control procedures. The original label was 'ser348ala' Tue Jun 30 16:03:18 BST 2020 This feature has been corrected as a result of our quality control procedures. The original label was 'p.Ser348Ala' physical association physical association The tyrosine 350 and Serine 348 hotspotsare in the transport signal motif SDYQRL (348-353) ap2m1-tgn41-4 1 4 unspecified role unspecified role prey prey region binding region binding-associated region binding region certain certain sequence position certain certain certain sequence position certain thioredoxin tag tag undetermined undetermined sequence position undetermined undetermined undetermined sequence position undetermined ecobb Escherichia coli (strain B / BL21) 5 unspecified role unspecified role bait bait P19814:p.Tyr350Ala mutation decreasing mutation decreasing interaction hotspot hotspot mutation decreasing certain certain sequence position certain certain certain sequence position certain Y A Wed May 02 15:15:50 BST 2018 This feature has been corrected as a result of our quality control procedures. The original label was 'tyr350ala' Tue Jun 30 15:40:47 BST 2020 This feature has been corrected as a result of our quality control procedures. The original label was 'p.Tyr350Ala' cytoplasmic domain binding region binding-associated region binding region certain certain sequence position certain certain certain sequence position certain P19814:p.Ser348Ala mutation decreasing mutation decreasing interaction hotspot hotspot mutation decreasing mutation analysis mutation analysis certain certain sequence position certain certain certain sequence position certain S A Wed May 02 18:40:31 BST 2018 This feature has been corrected as a result of our quality control procedures. The original label was 'ser348ala' Tue Jun 30 17:03:58 BST 2020 This feature has been corrected as a result of our quality control procedures. The original label was 'p.Ser348Ala' 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 The tyrosine 350 and Serine 348 hotspots are in the transport signal motif SDYQRL (348-353) Both bait and prey are purified. ap2m1-tgn41-5 2 5 unspecified role unspecified role bait bait cytoplasmic domain binding region binding-associated region binding region certain certain sequence position certain certain certain sequence position certain P19814:p.Ser348Ala mutation decreasing mutation decreasing interaction hotspot hotspot mutation decreasing mutation analysis mutation analysis certain certain sequence position certain certain certain sequence position certain S A Wed May 02 14:42:29 BST 2018 This feature has been corrected as a result of our quality control procedures. The original label was 'ser348ala' Tue Jun 30 16:51:52 BST 2020 This feature has been corrected as a result of our quality control procedures. The original label was 'p.Ser348Ala' 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 P19814:p.Tyr350Ala mutation decreasing mutation decreasing interaction hotspot hotspot mutation decreasing certain certain sequence position certain certain certain sequence position certain Y A Wed May 02 20:25:41 BST 2018 This feature has been corrected as a result of our quality control procedures. The original label was 'tyr350ala' Tue Jun 30 20:13:53 BST 2020 This feature has been corrected as a result of our quality control procedures. The original label was 'p.Tyr350Ala' ecobb Escherichia coli (strain B / BL21) 4 unspecified role unspecified role prey prey region binding region binding-associated region binding region certain certain sequence position certain certain certain sequence position certain thioredoxin tag tag undetermined undetermined sequence position undetermined undetermined undetermined sequence position undetermined ecobb Escherichia coli (strain B / BL21) physical association physical association The tyrosine 350 and Serine 348 hotspots are in the transport signal motif SDYQRL (348-353) Both bait and prey are purified. The affinity between TGN38 cytoplasmic tail and the mutant Y350A adaptin mu2 mutant is kd = 7.55 10-7 M The affinity between TGN38 cytoplasmic tail and the mutant S348A adaptin mu2 mutant is kd = 1.03 10-7 M