mbinfo MBInfo http://www.mechanobio.info/ The RAC binding domain/IRSp53-MIM homology domain of IRSp53 induces RAC-dependent membrane deformation. The RAC binding domain/IRSp53-MIM homology domain of IRSp53 induces RAC-dependent membrane deformation. J. Biol. Chem. (0021-9258) 2006 imex curation Suetsugu S., Murayama K., Sakamoto A., Hanawa-Suetsugu K., Seto A., Oikawa T., Mishima C., Shirouzu M., Takenawa T., Yokoyama S. Interaction detection: GST pull down. Participant detection: western blot results were quantitated by densitometry. The source of Rac1 traced from references [PMID: 7476445] and the source of IRSp53 specified by the author. yokoyama@biochem.s.u-tokyo.ac.jp 11-Oct-2012: Contacted by IntAct-Help. Only protein-protein interactions in vitro In vitro pull down pull down western blot western blot Immuno blot Immuno blot Suetsugu S., Murayama K., Sakamoto A., Hanawa-Suetsugu K., Seto A., Oikawa T., Mishima C., Shirouzu M., Takenawa T., Yokoyama S. Interaction detection: GST pull down. Participant detection: western blot results were quantitated by densitometry. The source of Rac1 traced from references [PMID: 7476445] and the source of IRSp53 specified by the author. yokoyama@biochem.s.u-tokyo.ac.jp Accepted 2012-SEP-21 by ORCHARD 11-Oct-2012: Contacted by IntAct-Help. J. Biol. Chem. (0021-9258) 2006 Only protein-protein interactions imex curation The RAC binding domain/IRSp53-MIM homology domain of IRSp53 induces RAC-dependent membrane deformation. The RAC binding domain/IRSp53-MIM homology domain of IRSp53 induces RAC-dependent membrane deformation. J. Biol. Chem. (0021-9258) 2006 imex curation Suetsugu S., Murayama K., Sakamoto A., Hanawa-Suetsugu K., Seto A., Oikawa T., Mishima C., Shirouzu M., Takenawa T., Yokoyama S. Interaction detection: GST pull down. Participant detection: western blot results were quantitated by densitometry. The source of Rac1 traced from references [PMID: 7476445] and the source of IRSp53 specified by the author. yokoyama@biochem.s.u-tokyo.ac.jp 11-Oct-2012: Contacted by IntAct-Help. Only protein-protein interactions in vitro In vitro biosensor biosensor predetermined predetermined participant predetermined Suetsugu S., Murayama K., Sakamoto A., Hanawa-Suetsugu K., Seto A., Oikawa T., Mishima C., Shirouzu M., Takenawa T., Yokoyama S. Interaction detection: GST pull down. Participant detection: western blot results were quantitated by densitometry. The source of Rac1 traced from references [PMID: 7476445] and the source of IRSp53 specified by the author. yokoyama@biochem.s.u-tokyo.ac.jp Accepted 2012-SEP-21 by ORCHARD 11-Oct-2012: Contacted by IntAct-Help. J. Biol. Chem. (0021-9258) 2006 Only protein-protein interactions imex curation rac1_human Ras-related C3 botulinum toxin substrate 1 RAC1 MIG5 p21-Rac1 Ras-like protein TC25 Cell migration-inducing gene 5 protein TC25 protein protein human Homo sapiens Human MQAIKCVVVGDGAVGKTCLLISYTTNAFPGEYIPTVFDNYSANVMVDGKPVNLGLWDTAGQEDYDRLRPLSYPQTDVFLICFSLVSPASFENVRAKWYPEVRHHCPNTPIILVGTKLDLRDDKDTIEKLKEKKLTPITYPQGLAMAKEIGAVKYLECSALTQRGLKTVFDEAIRAVLCPPPVKKRKRKCLLL ACEDF83A45E5EA67 baip2_human Brain-specific angiogenesis inhibitor 1-associated protein 2 Insulin receptor substrate protein of 53 kDa Insulin receptor substrate p53/p58 Fas ligand-associated factor 3 BAIAP2 protein protein human Homo sapiens Human MSLSRSEEMHRLTENVYKTIMEQFNPSLRNFIAMGKNYEKALAGVTYAAKGYFDALVKMGELASESQGSKELGDVLFQMAEVHRQIQNQLEEMLKSFHNELLTQLEQKVELDSRYLSAALKKYQTEQRSKGDALDKCQAELKKLRKKSQGSKNPQKYSDKELQYIDAISNKQGELENYVSDGYKTALTEERRRFCFLVEKQCAVAKNSAAYHSKGKELLAQKLPLWQQACADPSKIPERAVQLMQQVASNGATLPSALSASKSNLVISDPIPGAKPLPVPPELAPFVGRMSAQESTPIMNGVTGPDGEDYSPWADRKAAQPKSLSPPQSQSKLSDSYSNTLPVRKSVTPKNSYATTENKTLPRSSSMAAGLERNGRMRVKAIFSHAAGDNSTLLSFKEGDLITLLVPEARDGWHYGESEKTKMRGWFPFSYTRVLDSDGSDRLHMSLQQGKSSSTGNLLDKDDLAIPPPDYGAASRAFPAQTASGFKQRPYSVAVPAFSQGLDDYGARSMSRNPFAHVQLKPTVTNDRCDLSAQGPEGREHGDGSARTLAGR DIP protein Q9UQB8 original sequence version: 87 3B9EDC6405DCC99D baiap2-rac1-2 1 4 unspecified role unspecified role bait bait Q9UQB8:p.Lys143Glu mutation decreasing strength mutation decreasing interaction strength mutation decreasing strength mutation analysis mutation analysis certain certain sequence position certain certain certain sequence position certain K E Wed May 02 17:54:30 BST 2018 This feature has been corrected as a result of our quality control procedures. The original label was 'lys143glu' Tue Jun 30 19:12:12 BST 2020 This feature has been corrected as a result of our quality control procedures. The original label was 'p.Lys143Glu' Q9UQB8:p.[Arg11Glu;Gln23Glu] mutation decreasing strength mutation decreasing interaction strength mutation decreasing strength mutation analysis mutation analysis certain certain sequence position certain certain certain sequence position certain R E certain certain sequence position certain certain certain sequence position certain Q E Wed May 02 17:11:12 BST 2018 This feature has been corrected as a result of our quality control procedures. The original label was 'arg11glu,gln23glu' Tue Jun 30 16:07:26 BST 2020 This feature has been corrected as a result of our quality control procedures. The original label was 'p.[Arg11Glu;Gln23Glu]' Q9UQB8:p.[Lys143Glu;Lys147Glu] mutation decreasing strength mutation decreasing interaction strength mutation decreasing strength mutation analysis mutation analysis certain certain sequence position certain certain certain sequence position certain K E certain certain sequence position certain certain certain sequence position certain K E Wed May 02 14:53:05 BST 2018 This feature has been corrected as a result of our quality control procedures. The original label was 'lys143glu,lys147glu' Tue Jun 30 20:18:02 BST 2020 This feature has been corrected as a result of our quality control procedures. The original label was 'p.[Lys143Glu;Lys147Glu]' Q9UQB8:p.Gln23Glu mutation decreasing strength mutation decreasing interaction strength mutation decreasing strength mutation analysis mutation analysis certain certain sequence position certain certain certain sequence position certain Q E Wed May 02 16:27:09 BST 2018 This feature has been corrected as a result of our quality control procedures. The original label was 'gln23glu' Tue Jun 30 18:05:17 BST 2020 This feature has been corrected as a result of our quality control procedures. The original label was 'p.Gln23Glu' n-terminal region gst tag glutathione s tranferase tag glutathione S-tranferase tag glutathione S-tranferase tag gst tag n-term range n-terminal range n-term range n-term range n-terminal range n-term range Q9UQB8:p.[Lys142Ala;Lys143Ala;Arg145Ala;Lys146Ala;Lys147Ala] mutation decreasing strength mutation decreasing interaction strength mutation decreasing strength alanine scanning alanine scanning certain certain sequence position certain certain certain sequence position certain K A certain certain sequence position certain certain certain sequence position certain K A certain certain sequence position certain certain certain sequence position certain R A certain certain sequence position certain certain certain sequence position certain K A certain certain sequence position certain certain certain sequence position certain K A Wed May 02 16:47:11 BST 2018 This feature has been corrected as a result of our quality control procedures. The original label was 'lys142ala,lys143ala,arg145ala,lys146ala,lys147ala' Tue Jun 30 17:00:36 BST 2020 This feature has been corrected as a result of our quality control procedures. The original label was 'p.[Lys142Ala;Lys143Ala;Arg145Ala;Lys146Ala;Lys147Ala]' ecoli Escherichia coli (strain K12) 3 unspecified role unspecified role prey prey ecoli Escherichia coli (strain K12) physical association physical association Fig 2E. Rac1 was GTPgammaS-loaded. baiap2-rac1-3 2 4 unspecified role unspecified role bait bait rcb domain sufficient to bind sufficient binding region sufficient to bind certain certain sequence position certain certain certain sequence position certain n-terminal region gst tag glutathione s tranferase tag glutathione S-tranferase tag glutathione S-tranferase tag gst tag n-term range n-terminal range n-term range n-term range n-terminal range n-term range ecoli Escherichia coli (strain K12) 3 unspecified role unspecified role prey prey ecoli Escherichia coli (strain K12) physical association physical association Fig 3B. IRSp53-RCB bound strongly only to the GTPgammaS-loaded Rac1. The interaction was greatly decreased with GDP-loaded Rac1.