UniProt UniProt http://www.uniprot.org Interaction of the RAGE cytoplasmic domain with diaphanous-1 is required for ligand-stimulated cellular migration through activation of Rac1 and Cdc42. Interaction of the RAGE cytoplasmic domain with diaphanous-1 is required for ligand-stimulated cellular migration through activation of Rac1 and Cdc42. The Journal of biological chemistry 2008 imex curation Hudson BI., Kalea AZ., Del Mar Arriero M., Harja E., Boulanger E., D'Agati V., Schmidt AM. DIAPH1 sequence coordinates for binding sites have been adapted to UniProt. Cloned full length human DIAPH1 cannot be mapped toan UniProt isoform hence has been mapped to the canonical form. bh2021@columbia.edu 17-Sep-2015: Contacted by IntAct-Help. Only protein-protein interactions rat-c6 Rattus norvegicus c6 Rat glial tumour confocal microscopy confocal microscopy immunostaining immunostaining Hudson BI., Kalea AZ., Del Mar Arriero M., Harja E., Boulanger E., D'Agati V., Schmidt AM. DIAPH1 sequence coordinates for binding sites have been adapted to UniProt. Cloned full length human DIAPH1 cannot be mapped toan UniProt isoform hence has been mapped to the canonical form. bh2021@columbia.edu Accepted 2015-JUL-30 by ORCHARD The Journal of biological chemistry 2008 IMEx imex curation Interaction of the RAGE cytoplasmic domain with diaphanous-1 is required for ligand-stimulated cellular migration through activation of Rac1 and Cdc42. Interaction of the RAGE cytoplasmic domain with diaphanous-1 is required for ligand-stimulated cellular migration through activation of Rac1 and Cdc42. The Journal of biological chemistry 2008 imex curation Hudson BI., Kalea AZ., Del Mar Arriero M., Harja E., Boulanger E., D'Agati V., Schmidt AM. DIAPH1 sequence coordinates for binding sites have been adapted to UniProt. Cloned full length human DIAPH1 cannot be mapped toan UniProt isoform hence has been mapped to the canonical form. bh2021@columbia.edu 17-Sep-2015: Contacted by IntAct-Help. Only protein-protein interactions rat-c6 Rattus norvegicus c6 Rat glial tumour anti bait coip anti bait coimmunoprecipitation anti bait coip western blot western blot Immuno blot Immuno blot Hudson BI., Kalea AZ., Del Mar Arriero M., Harja E., Boulanger E., D'Agati V., Schmidt AM. DIAPH1 sequence coordinates for binding sites have been adapted to UniProt. Cloned full length human DIAPH1 cannot be mapped toan UniProt isoform hence has been mapped to the canonical form. bh2021@columbia.edu Accepted 2015-JUL-22 by ORCHARD The Journal of biological chemistry 2008 IMEx imex curation Interaction of the RAGE cytoplasmic domain with diaphanous-1 is required for ligand-stimulated cellular migration through activation of Rac1 and Cdc42. Interaction of the RAGE cytoplasmic domain with diaphanous-1 is required for ligand-stimulated cellular migration through activation of Rac1 and Cdc42. The Journal of biological chemistry 2008 imex curation Hudson BI., Kalea AZ., Del Mar Arriero M., Harja E., Boulanger E., D'Agati V., Schmidt AM. DIAPH1 sequence coordinates for binding sites have been adapted to UniProt. Cloned full length human DIAPH1 cannot be mapped toan UniProt isoform hence has been mapped to the canonical form. bh2021@columbia.edu 17-Sep-2015: Contacted by IntAct-Help. Only protein-protein interactions in vitro In vitro pull down pull down western blot western blot Immuno blot Immuno blot Hudson BI., Kalea AZ., Del Mar Arriero M., Harja E., Boulanger E., D'Agati V., Schmidt AM. DIAPH1 sequence coordinates for binding sites have been adapted to UniProt. Cloned full length human DIAPH1 cannot be mapped toan UniProt isoform hence has been mapped to the canonical form. bh2021@columbia.edu Accepted 2015-JUL-22 by ORCHARD The Journal of biological chemistry 2008 IMEx imex curation Interaction of the RAGE cytoplasmic domain with diaphanous-1 is required for ligand-stimulated cellular migration through activation of Rac1 and Cdc42. Interaction of the RAGE cytoplasmic domain with diaphanous-1 is required for ligand-stimulated cellular migration through activation of Rac1 and Cdc42. The Journal of biological chemistry 2008 imex curation Hudson BI., Kalea AZ., Del Mar Arriero M., Harja E., Boulanger E., D'Agati V., Schmidt AM. DIAPH1 sequence coordinates for binding sites have been adapted to UniProt. Cloned full length human DIAPH1 cannot be mapped toan UniProt isoform hence has been mapped to the canonical form. bh2021@columbia.edu 17-Sep-2015: Contacted by IntAct-Help. Only protein-protein interactions human-skbr3 Homo sapiens SKBR3 skbr3 SKBR3 Species: human; Tissue: breast; Tumor: adenocarcinoma; Derived from: metastatic site: pleural effusion anti tag coip anti tag coimmunoprecipitation anti tag coip anti tag western anti tag western blot anti tag western Hudson BI., Kalea AZ., Del Mar Arriero M., Harja E., Boulanger E., D'Agati V., Schmidt AM. DIAPH1 sequence coordinates for binding sites have been adapted to UniProt. Cloned full length human DIAPH1 cannot be mapped toan UniProt isoform hence has been mapped to the canonical form. bh2021@columbia.edu Accepted 2015-JUL-22 by ORCHARD The Journal of biological chemistry 2008 IMEx imex curation Interaction of the RAGE cytoplasmic domain with diaphanous-1 is required for ligand-stimulated cellular migration through activation of Rac1 and Cdc42. Interaction of the RAGE cytoplasmic domain with diaphanous-1 is required for ligand-stimulated cellular migration through activation of Rac1 and Cdc42. The Journal of biological chemistry 2008 imex curation Hudson BI., Kalea AZ., Del Mar Arriero M., Harja E., Boulanger E., D'Agati V., Schmidt AM. DIAPH1 sequence coordinates for binding sites have been adapted to UniProt. Cloned full length human DIAPH1 cannot be mapped toan UniProt isoform hence has been mapped to the canonical form. bh2021@columbia.edu 17-Sep-2015: Contacted by IntAct-Help. Only protein-protein interactions 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 nucleotide sequence nucleotide sequence identification sequence cloning sequence cloning nucleotide sequence Hudson BI., Kalea AZ., Del Mar Arriero M., Harja E., Boulanger E., D'Agati V., Schmidt AM. DIAPH1 sequence coordinates for binding sites have been adapted to UniProt. Cloned full length human DIAPH1 cannot be mapped toan UniProt isoform hence has been mapped to the canonical form. bh2021@columbia.edu Accepted 2015-JUL-22 by ORCHARD human lung cDNA The Journal of biological chemistry 2008 IMEx imex curation diap1_rat Protein diaphanous homolog 1 Diaph1 Diap1 Diaphanous-related formin-1 mDIA1 protein protein rat Rattus norvegicus (Rat) Rat MEPSGGGLGPGRGTRDKKKGRSPDELPATGGDGGKHKKFTLKRLMADELERFTSMRIKKEKEKPNSAHRNSSASYGDDPTAQSLQDISDDQVLVLFEQMLVDMNLNEEKQQPLREKDIVIKREMVSQYLHTSKAGMNQKESSRSAMMYIQELRSGLRDMHLLSCLESLRVSLNNNPVSWVQTFGAEGLASLLDILKRLHDEKEETSGNYDSRNQHEIIRCLKAFMNNKFGIKTMLETEEGILLLVRAMDPAVPNMMIDAAKLLSALCILPQPEDMNERVLEAMTERAEMEEVERFQPLLDGLKSGTSIALKVGCLQLINALITPAEELDFRVHIRSELMRLGLHQVLQELREIDNDDMRVQLNVFDEQGDEDFFDLKGRLDDIRMEMDDFGEVFQIILNTVKDSKAEPHFLSILQHLLLVRNDYEARPQYYKLIEECVSQIVLHKNGTDPDFKCRHLQIDIEGLVDQMIDKTKVEKSEAKATELEKKLDSELTARHELQVEMKKMENDFEQKLQDLQGEKDALDSEKQQITTQKQDLEAEVSKLTGEVAKLSKELEDAKKEMASLSAVAVAPSVSSSAAVPQAPPLPGTSGTVIPPPPPPPLPGGAVPPPPPPPLPAGTGIPPPPPLPGGACISSSPQLFGSTAIPPPPPLPGATAIPPPPPLPGDTAIPPPPPLPGXTAIPPPPPLPGATGVPPPPPPLPGSVGVPPPPPLPGGPGLPPPPPPFPGAPGIPPPPPGMGVPPPPPFGFGIPAAPVLPFGLTPKKVYKPEVQLRRPNWSKFVAEDLSQDCFWTKVKEDRFENNELFAKLTLAFSAQTKTSLAKKDQEGGEEKKSVQKKKVKELKVLDSKTAQNLSIFLGSFRMPYQEIKNVILEVNEAVLTESMIQNLIKQMPEPEQLKMLSELKEEYDDLAESEQFGVVMGTVPRLRPRLNAILFKLQFSEQVENIKPEIVSVTAACEELRKSENFSSLLELTLLVGNYMNAGSRNAGAFGFNISFLCKLRDTKSADQKMTLLHFLAELCETDHPDVLKFPDELAHVEKASRVSAENLQKNLDQMKKQIADVERDVQNFPAATDEKDKFVEKMTSFVKDAQEQYNKLRMMHSNMETLYKELGDYFVFDPKKLSVEEFFMDLHNFRNMFLQAVKENQKRRETEEKMRRAKLAKEKAEKERLEKQQKREQLIDMNAEGDETGVMDSLLEALQSGAAFRRKRGPRQVNRKAGCAVTSLLASELTKDDAVAASSAKVPKKSEGVTTILEEAKELVGRAS 552D8D90F2FE5E0D rage_rat Advanced glycosylation end product-specific receptor Ager Rage Receptor for advanced glycosylation end products protein protein rat Rattus norvegicus (Rat) Rat MPTGTVARAWVLVLALWGAVAGGQNITARIGEPLMLSCKGAPKKPTQKLEWKLNTGRTEAWKVLSPQGDPWDSVARILPNGSLLLPAIGIVDEGTFRCRATNRLGKEVKSNYRVRVYQIPGKPEIVNPASELTANVPNKVGTCVSEGSYPAGTLSWHLDGKPLIPDGKGTVVKEETRRHPETGLFTLRSELTVTPAQGGTTPTYSCSFSLGLPRRRPLNTAPIQPRVREPLPPEGIQLLVEPEGGTVAPGGTVTLTCAISAQPPPQIHWIKDGTPLPLAPSPVLLLPEVGHEDEGIYSCVATHPSHGPQESPPVNIRVTETGDEGQAAGSVDGSGLGTLALALGILGGLGIAALLIGAILWRKRQPRLEERKAPESQEDEEERAELNQSEEAEMPENGAGGP 594481BC3A51E94E rage_human Advanced glycosylation end product-specific receptor AGER RAGE Receptor for advanced glycosylation end products protein protein human Homo sapiens Human MAAGTAVGAWVLVLSLWGAVVGAQNITARIGEPLVLKCKGAPKKPPQRLEWKLNTGRTEAWKVLSPQGGGPWDSVARVLPNGSLFLPAVGIQDEGIFRCQAMNRNGKETKSNYRVRVYQIPGKPEIVDSASELTAGVPNKVGTCVSEGSYPAGTLSWHLDGKPLVPNEKGVSVKEQTRRHPETGLFTLQSELMVTPARGGDPRPTFSCSFSPGLPRHRALRTAPIQPRVWEPVPLEEVQLVVEPEGGAVAPGGTVTLTCEVPAQPSPQIHWMKDGVPLPLPPSPVLILPEIGPQDQGTYSCVATHSSHGPQESRAVSISIIEPGEEGPTAGSVGGSGLGTLALALGILGGLGTAALLIGVILWQRRQRRGEERKAPENQEEEEERAELNQSEEPEAGESSTGGP DIP protein Q15109 original sequence version: 157 0D584C436C30CCE7 diap1_human Protein diaphanous homolog 1 DIAPH1 DIAP1 Diaphanous-related formin-1 protein protein human Homo sapiens Human MEPPGGSLGPGRGTRDKKKGRSPDELPSAGGDGGKSKKFTLKRLMADELERFTSMRIKKEKEKPNSAHRNSSASYGDDPTAQSLQDVSDEQVLVLFEQMLLDMNLNEEKQQPLREKDIIIKREMVSQYLYTSKAGMSQKESSKSAMMYIQELRSGLRDMPLLSCLESLRVSLNNNPVSWVQTFGAEGLASLLDILKRLHDEKEETAGSYDSRNKHEIIRCLKAFMNNKFGIKTMLETEEGILLLVRAMDPAVPNMMIDAAKLLSALCILPQPEDMNERVLEAMTERAEMDEVERFQPLLDGLKSGTTIALKVGCLQLINALITPAEELDFRVHIRSELMRLGLHQVLQDLREIENEDMRVQLNVFDEQGEEDSYDLKGRLDDIRMEMDDFNEVFQILLNTVKDSKAEPHFLSILQHLLLVRNDYEARPQYYKLIEECISQIVLHKNGADPDFKCRHLQIEIEGLIDQMIDKTKVEKSEAKAAELEKKLDSELTARHELQVEMKKMESDFEQKLQDLQGEKDALHSEKQQIATEKQDLEAEVSQLTGEVAKLTKELEDAKKEMASLSAAAITVPPSVPSRAPVPPAPPLPGDSGTIIPPPPAPGDSTTPPPPPPPPPPPPPLPGGVCISSPPSLPGGTAISPPPPLSGDATIPPPPPLPEGVGIPSPSSLPGGTAIPPPPPLPGSARIPPPPPPLPGSAGIPPPPPPLPGEAGMPPPPPPLPGGPGIPPPPPFPGGPGIPPPPPGMGMPPPPPFGFGVPAAPVLPFGLTPKKLYKPEVQLRRPNWSKLVAEDLSQDCFWTKVKEDRFENNELFAKLTLTFSAQTKTSKAKKDQEGGEEKKSVQKKKVKELKVLDSKTAQNLSIFLGSFRMPYQEIKNVILEVNEAVLTESMIQNLIKQMPEPEQLKMLSELKDEYDDLAESEQFGVVMGTVPRLRPRLNAILFKLQFSEQVENIKPEIVSVTAACEELRKSESFSNLLEITLLVGNYMNAGSRNAGAFGFNISFLCKLRDTKSTDQKMTLLHFLAELCENDYPDVLKFPDELAHVEKASRVSAENLQKNLDQMKKQISDVERDVQNFPAATDEKDKFVEKMTSFVKDAQEQYNKLRMMHSNMETLYKELGEYFLFDPKKLSVEEFFMDLHNFRNMFLQAVKENQKRRETEEKMRRAKLAKEKAEKERLEKQQKREQLIDMNAEGDETGVMDSLLEALQSGAAFRRKRGPRQANRKAGCAVTSLLASELTKDDAMAAVPAKVSKNSETFPTILEEAKELVGRAS 9C8273DE4748564F ager-diaph1-1 5 9 unspecified role unspecified role prey prey region sufficient to bind sufficient binding region sufficient to bind certain certain sequence position certain certain certain sequence position certain 8 unspecified role unspecified role bait bait region sufficient to bind sufficient binding region sufficient to bind certain certain sequence position certain certain certain sequence position certain 12 14 physical association physical association no figure diaph1-ager-1 3 9 unspecified role unspecified role prey prey rabit-reticulocyte Oryctolagus cuniculus reticulocyte reticulocyte Reticulocytes 8 unspecified role unspecified role bait bait region sufficient to bind sufficient binding region sufficient to bind certain certain sequence position certain certain certain sequence position certain ecoli Escherichia coli (strain K12) physical association physical association 2A ager-diaph1-2 4 9 unspecified role unspecified role prey prey n-terminus myc tag myc tag EUKLISEED epitope tag EUKLISEED epitope tag n-term range n-terminal range n-term range n-term range n-terminal range n-term range formin_homolog_ 1 sufficient to bind sufficient binding region sufficient to bind certain certain sequence position certain certain certain sequence position certain 8 unspecified role unspecified role bait bait region sufficient to bind sufficient binding region sufficient to bind certain certain sequence position certain certain certain sequence position certain n-terminus his tag his tag Hexa-His-tag 6-His-tag Histidine-tag Hexa-His-tag Histidine-tag 6-His-tag n-term range n-terminal range n-term range n-term range n-terminal range n-term range 22 24 physical association physical association 2B and 4B diaph1-1 2 8 unspecified role unspecified role bait bait nucl transfection nucleic acid transfection nucl transfection region required to bind necessary binding region required to bind certain certain sequence position certain certain certain sequence position certain 6 unspecified role unspecified role prey prey cell lysate cell lysate physical association physical association 2C ager-diaph1-3 1 8 unspecified role unspecified role neutral component neutral component nucl transfection nucleic acid transfection nucl transfection 6 unspecified role unspecified role neutral component neutral component colocalization colocalization 3A ager-diaph1-4 1 7 unspecified role unspecified role neutral component neutral component 6 unspecified role unspecified role neutral component neutral component colocalization colocalization 3B