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/ Structural basis of the junctional anchorage of the cerebral cavernous malformations complex. Structural basis of the junctional anchorage of the cerebral cavernous malformations complex. The Journal of cell biology 2012 imex curation Gingras AR., Liu JJ., Ginsberg MH., Gingras AR., Liu JJ., Ginsberg MH., Gingras AR., Liu JJ., Ginsberg MH., Gingras AR., Liu JJ., Ginsberg MH. Dark Space from Sandra no52? KRIT1 FERM domain numbering found in PMID: 17954608, as were details of constructs used. ude.dscu@grebsnighm Only protein-protein interactions in vitro In vitro pull down pull down experimental particp experimental participant identification experimental particp Gingras AR., Liu JJ., Ginsberg MH., Gingras AR., Liu JJ., Ginsberg MH., Gingras AR., Liu JJ., Ginsberg MH., Gingras AR., Liu JJ., Ginsberg MH. Dark Space from Sandra no52? Bound proteins were analyzed by immunoblotting or Coomassie blue staining. KRIT1 FERM domain numbering found in PMID: 17954608, as were details of constructs used. ude.dscu@grebsnighm Accepted 2017-FEB-02 AT 14:41 GMT AT 14:41 GMT by ORCHARD The Journal of cell biology 2012 imex curation With regard to your comment from Expt-2:- " Fig. 1B Methodology is given in the M&M - its anti-GFP, so Krit1 is the bait + immunoblotting (anti-tag I think as no mention of anti-Heg)." However HEG1 TAIL proteins/peptides were used here - so this must be an "In Vitro" assay- there is nothing in the methods mentioning GFP- IP and also using TAIL proteins - so I would doubt this is an anti-tag IP. (although I agree Participant Detection is most likely Anti-Tag WB) I have altered as you suggest (Bait-Prey reversal) but I dont think this is correct- I think this is an "In Vitro protein Interaction Assay" - Pulldown, as entered before. Quite possibly it could be a Streptavidin Pulldown - as an N-terminal biotinylation tag is present as well as a His tag. (also E.coli expressed proteins) With regard to your comment:-"EBI-12734468 - the shorter cytoplasmic tail, do you mean 'required to bind'? " - No - I meant this to be "binding region" as the text states "In contrast, removal of 19 residues 1,363–1,381 at the C terminus of HEG1 (HEG1 delta1,363) drastically reduced KRIT1 binding.." - so this implies there is still some binding, - looking at the image there is still a large "blob" present, how much non-specific binding I would not like to say, so I thought better to leave as a "binding region".; Please see new Expt (-7) for comments on fig 1B. Mutations added to fig 4D.; Altered as suggested; altered as suggested Structural basis of the junctional anchorage of the cerebral cavernous malformations complex. Structural basis of the junctional anchorage of the cerebral cavernous malformations complex. The Journal of cell biology 2012 imex curation Gingras AR., Liu JJ., Ginsberg MH., Gingras AR., Liu JJ., Ginsberg MH., Gingras AR., Liu JJ., Ginsberg MH., Gingras AR., Liu JJ., Ginsberg MH. Dark Space from Sandra no52? KRIT1 FERM domain numbering found in PMID: 17954608, as were details of constructs used. ude.dscu@grebsnighm Only protein-protein interactions 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. anti tag coip anti tag coimmunoprecipitation anti tag coip western blot western blot Immuno blot Immuno blot Gingras AR., Liu JJ., Ginsberg MH., Gingras AR., Liu JJ., Ginsberg MH., Gingras AR., Liu JJ., Ginsberg MH., Gingras AR., Liu JJ., Ginsberg MH. Dark Space from Sandra no52? KRIT1 FERM domain numbering found in PMID: 17954608, as were details of constructs used. ude.dscu@grebsnighm Accepted 2017-FEB-02 AT 14:41 GMT AT 14:41 GMT by ORCHARD The Journal of cell biology 2012 imex curation With regard to your comment from Expt-2:- " Fig. 1B Methodology is given in the M&M - its anti-GFP, so Krit1 is the bait + immunoblotting (anti-tag I think as no mention of anti-Heg)." However HEG1 TAIL proteins/peptides were used here - so this must be an "In Vitro" assay- there is nothing in the methods mentioning GFP- IP and also using TAIL proteins - so I would doubt this is an anti-tag IP. (although I agree Participant Detection is most likely Anti-Tag WB) I have altered as you suggest (Bait-Prey reversal) but I dont think this is correct- I think this is an "In Vitro protein Interaction Assay" - Pulldown, as entered before. Quite possibly it could be a Streptavidin Pulldown - as an N-terminal biotinylation tag is present as well as a His tag. (also E.coli expressed proteins) With regard to your comment:-"EBI-12734468 - the shorter cytoplasmic tail, do you mean 'required to bind'? " - No - I meant this to be "binding region" as the text states "In contrast, removal of 19 residues 1,363–1,381 at the C terminus of HEG1 (HEG1 delta1,363) drastically reduced KRIT1 binding.." - so this implies there is still some binding, - looking at the image there is still a large "blob" present, how much non-specific binding I would not like to say, so I thought better to leave as a "binding region".; Please see new Expt (-7) for comments on fig 1B. Mutations added to fig 4D.; Altered as suggested; altered as suggested Structural basis of the junctional anchorage of the cerebral cavernous malformations complex. Structural basis of the junctional anchorage of the cerebral cavernous malformations complex. The Journal of cell biology 2012 imex curation Gingras AR., Liu JJ., Ginsberg MH., Gingras AR., Liu JJ., Ginsberg MH., Gingras AR., Liu JJ., Ginsberg MH., Gingras AR., Liu JJ., Ginsberg MH. Dark Space from Sandra no52? KRIT1 FERM domain numbering found in PMID: 17954608, as were details of constructs used. ude.dscu@grebsnighm Only protein-protein interactions in vitro In vitro affinity chrom affinity chromatography technology Affinity purification Affinity purification affinity chrom anti tag western anti tag western blot anti tag western Gingras AR., Liu JJ., Ginsberg MH., Gingras AR., Liu JJ., Ginsberg MH., Gingras AR., Liu JJ., Ginsberg MH., Gingras AR., Liu JJ., Ginsberg MH. Dark Space from Sandra no52? Bound proteins were analyzed by immunoblotting or Coomassie blue staining. KRIT1 FERM domain numbering found in PMID: 17954608, as were details of constructs used. ude.dscu@grebsnighm Accepted 2017-FEB-02 AT 14:41 GMT AT 14:41 GMT by ORCHARD The Journal of cell biology 2012 imex curation With regard to your comment from Expt-2:- " Fig. 1B Methodology is given in the M&M - its anti-GFP, so Krit1 is the bait + immunoblotting (anti-tag I think as no mention of anti-Heg)." However HEG1 TAIL proteins/peptides were used here - so this must be an "In Vitro" assay- there is nothing in the methods mentioning GFP- IP and also using TAIL proteins - so I would doubt this is an anti-tag IP. (although I agree Participant Detection is most likely Anti-Tag WB) I have altered as you suggest (Bait-Prey reversal) but I dont think this is correct- I think this is an "In Vitro protein Interaction Assay" - Pulldown, as entered before. Quite possibly it could be a Streptavidin Pulldown - as an N-terminal biotinylation tag is present as well as a His tag. (also E.coli expressed proteins) With regard to your comment:-"EBI-12734468 - the shorter cytoplasmic tail, do you mean 'required to bind'? " - No - I meant this to be "binding region" as the text states "In contrast, removal of 19 residues 1,363–1,381 at the C terminus of HEG1 (HEG1 delta1,363) drastically reduced KRIT1 binding.." - so this implies there is still some binding, - looking at the image there is still a large "blob" present, how much non-specific binding I would not like to say, so I thought better to leave as a "binding region".; Please see new Expt (-7) for comments on fig 1B. Mutations added to fig 4D.; Altered as suggested; altered as suggested Structural basis of the junctional anchorage of the cerebral cavernous malformations complex. Structural basis of the junctional anchorage of the cerebral cavernous malformations complex. The Journal of cell biology 2012 imex curation Gingras AR., Liu JJ., Ginsberg MH., Gingras AR., Liu JJ., Ginsberg MH., Gingras AR., Liu JJ., Ginsberg MH., Gingras AR., Liu JJ., Ginsberg MH. Dark Space from Sandra no52? KRIT1 FERM domain numbering found in PMID: 17954608, as were details of constructs used. ude.dscu@grebsnighm Only protein-protein interactions in vitro In vitro pull down pull down weight by comassie molecular weight estimation by coomasie staining weight by comassie Gingras AR., Liu JJ., Ginsberg MH., Gingras AR., Liu JJ., Ginsberg MH., Gingras AR., Liu JJ., Ginsberg MH., Gingras AR., Liu JJ., Ginsberg MH. Dark Space from Sandra no52? KRIT1 FERM domain numbering found in PMID: 17954608, as were details of constructs used. ude.dscu@grebsnighm Accepted 2017-FEB-02 AT 14:41 GMT AT 14:41 GMT by ORCHARD The Journal of cell biology 2012 imex curation With regard to your comment from Expt-2:- " Fig. 1B Methodology is given in the M&M - its anti-GFP, so Krit1 is the bait + immunoblotting (anti-tag I think as no mention of anti-Heg)." However HEG1 TAIL proteins/peptides were used here - so this must be an "In Vitro" assay- there is nothing in the methods mentioning GFP- IP and also using TAIL proteins - so I would doubt this is an anti-tag IP. (although I agree Participant Detection is most likely Anti-Tag WB) I have altered as you suggest (Bait-Prey reversal) but I dont think this is correct- I think this is an "In Vitro protein Interaction Assay" - Pulldown, as entered before. Quite possibly it could be a Streptavidin Pulldown - as an N-terminal biotinylation tag is present as well as a His tag. (also E.coli expressed proteins) With regard to your comment:-"EBI-12734468 - the shorter cytoplasmic tail, do you mean 'required to bind'? " - No - I meant this to be "binding region" as the text states "In contrast, removal of 19 residues 1,363–1,381 at the C terminus of HEG1 (HEG1 delta1,363) drastically reduced KRIT1 binding.." - so this implies there is still some binding, - looking at the image there is still a large "blob" present, how much non-specific binding I would not like to say, so I thought better to leave as a "binding region".; Please see new Expt (-7) for comments on fig 1B. Mutations added to fig 4D.; Altered as suggested; altered as suggested Structural basis of the junctional anchorage of the cerebral cavernous malformations complex. Structural basis of the junctional anchorage of the cerebral cavernous malformations complex. The Journal of cell biology 2012 imex curation Gingras AR., Liu JJ., Ginsberg MH., Gingras AR., Liu JJ., Ginsberg MH., Gingras AR., Liu JJ., Ginsberg MH., Gingras AR., Liu JJ., Ginsberg MH. Dark Space from Sandra no52? KRIT1 FERM domain numbering found in PMID: 17954608, as were details of constructs used. ude.dscu@grebsnighm Only protein-protein interactions in vitro In vitro affinity chrom affinity chromatography technology Affinity purification Affinity purification affinity chrom western blot western blot Immuno blot Immuno blot Gingras AR., Liu JJ., Ginsberg MH., Gingras AR., Liu JJ., Ginsberg MH., Gingras AR., Liu JJ., Ginsberg MH., Gingras AR., Liu JJ., Ginsberg MH. Dark Space from Sandra no52? An affinity matrix with an immobilized synthetic HEG1 C-terminal 19-residue peptide or HEG1 deletion mutant lacking the two C-terminal aas was used. KRIT1 FERM domain numbering found in PMID: 17954608, as were details of constructs used. ude.dscu@grebsnighm Accepted 2017-FEB-02 AT 14:41 GMT AT 14:41 GMT by ORCHARD The Journal of cell biology 2012 imex curation With regard to your comment from Expt-2:- " Fig. 1B Methodology is given in the M&M - its anti-GFP, so Krit1 is the bait + immunoblotting (anti-tag I think as no mention of anti-Heg)." However HEG1 TAIL proteins/peptides were used here - so this must be an "In Vitro" assay- there is nothing in the methods mentioning GFP- IP and also using TAIL proteins - so I would doubt this is an anti-tag IP. (although I agree Participant Detection is most likely Anti-Tag WB) I have altered as you suggest (Bait-Prey reversal) but I dont think this is correct- I think this is an "In Vitro protein Interaction Assay" - Pulldown, as entered before. Quite possibly it could be a Streptavidin Pulldown - as an N-terminal biotinylation tag is present as well as a His tag. (also E.coli expressed proteins) With regard to your comment:-"EBI-12734468 - the shorter cytoplasmic tail, do you mean 'required to bind'? " - No - I meant this to be "binding region" as the text states "In contrast, removal of 19 residues 1,363–1,381 at the C terminus of HEG1 (HEG1 delta1,363) drastically reduced KRIT1 binding.." - so this implies there is still some binding, - looking at the image there is still a large "blob" present, how much non-specific binding I would not like to say, so I thought better to leave as a "binding region".; Please see new Expt (-7) for comments on fig 1B. Mutations added to fig 4D.; Altered as suggested; altered as suggested Structural basis of the junctional anchorage of the cerebral cavernous malformations complex. Structural basis of the junctional anchorage of the cerebral cavernous malformations complex. The Journal of cell biology 2012 imex curation Gingras AR., Liu JJ., Ginsberg MH., Gingras AR., Liu JJ., Ginsberg MH., Gingras AR., Liu JJ., Ginsberg MH., Gingras AR., Liu JJ., Ginsberg MH. Dark Space from Sandra no52? KRIT1 FERM domain numbering found in PMID: 17954608, as were details of constructs used. ude.dscu@grebsnighm Only protein-protein interactions in vitro In vitro itc isothermal titration calorimetry ITC ITC itc predetermined predetermined participant predetermined Gingras AR., Liu JJ., Ginsberg MH., Gingras AR., Liu JJ., Ginsberg MH., Gingras AR., Liu JJ., Ginsberg MH., Gingras AR., Liu JJ., Ginsberg MH. Dark Space from Sandra no52? KRIT1 FERM domain numbering found in PMID: 17954608, as were details of constructs used. ude.dscu@grebsnighm Accepted 2017-FEB-02 AT 14:41 GMT AT 14:41 GMT by ORCHARD The Journal of cell biology 2012 imex curation With regard to your comment from Expt-2:- " Fig. 1B Methodology is given in the M&M - its anti-GFP, so Krit1 is the bait + immunoblotting (anti-tag I think as no mention of anti-Heg)." However HEG1 TAIL proteins/peptides were used here - so this must be an "In Vitro" assay- there is nothing in the methods mentioning GFP- IP and also using TAIL proteins - so I would doubt this is an anti-tag IP. (although I agree Participant Detection is most likely Anti-Tag WB) I have altered as you suggest (Bait-Prey reversal) but I dont think this is correct- I think this is an "In Vitro protein Interaction Assay" - Pulldown, as entered before. Quite possibly it could be a Streptavidin Pulldown - as an N-terminal biotinylation tag is present as well as a His tag. (also E.coli expressed proteins) With regard to your comment:-"EBI-12734468 - the shorter cytoplasmic tail, do you mean 'required to bind'? " - No - I meant this to be "binding region" as the text states "In contrast, removal of 19 residues 1,363–1,381 at the C terminus of HEG1 (HEG1 delta1,363) drastically reduced KRIT1 binding.." - so this implies there is still some binding, - looking at the image there is still a large "blob" present, how much non-specific binding I would not like to say, so I thought better to leave as a "binding region".; Please see new Expt (-7) for comments on fig 1B. Mutations added to fig 4D.; Altered as suggested; altered as suggested Structural basis of the junctional anchorage of the cerebral cavernous malformations complex. Structural basis of the junctional anchorage of the cerebral cavernous malformations complex. The Journal of cell biology 2012 imex curation Gingras AR., Liu JJ., Ginsberg MH., Gingras AR., Liu JJ., Ginsberg MH., Gingras AR., Liu JJ., Ginsberg MH., Gingras AR., Liu JJ., Ginsberg MH. Dark Space from Sandra no52? KRIT1 FERM domain numbering found in PMID: 17954608, as were details of constructs used. ude.dscu@grebsnighm Only protein-protein interactions in vitro In vitro x-ray diffraction x-ray crystallography X-ray X-ray x-ray diffraction predetermined predetermined participant predetermined Gingras AR., Liu JJ., Ginsberg MH., Gingras AR., Liu JJ., Ginsberg MH., Gingras AR., Liu JJ., Ginsberg MH., Gingras AR., Liu JJ., Ginsberg MH. Dark Space from Sandra no52? KRIT1 FERM domain numbering found in PMID: 17954608, as were details of constructs used. ude.dscu@grebsnighm Accepted 2017-FEB-02 AT 14:41 GMT AT 14:41 GMT by ORCHARD The Journal of cell biology 2012 imex curation With regard to your comment from Expt-2:- " Fig. 1B Methodology is given in the M&M - its anti-GFP, so Krit1 is the bait + immunoblotting (anti-tag I think as no mention of anti-Heg)." However HEG1 TAIL proteins/peptides were used here - so this must be an "In Vitro" assay- there is nothing in the methods mentioning GFP- IP and also using TAIL proteins - so I would doubt this is an anti-tag IP. (although I agree Participant Detection is most likely Anti-Tag WB) I have altered as you suggest (Bait-Prey reversal) but I dont think this is correct- I think this is an "In Vitro protein Interaction Assay" - Pulldown, as entered before. Quite possibly it could be a Streptavidin Pulldown - as an N-terminal biotinylation tag is present as well as a His tag. (also E.coli expressed proteins) With regard to your comment:-"EBI-12734468 - the shorter cytoplasmic tail, do you mean 'required to bind'? " - No - I meant this to be "binding region" as the text states "In contrast, removal of 19 residues 1,363–1,381 at the C terminus of HEG1 (HEG1 delta1,363) drastically reduced KRIT1 binding.." - so this implies there is still some binding, - looking at the image there is still a large "blob" present, how much non-specific binding I would not like to say, so I thought better to leave as a "binding region".; Please see new Expt (-7) for comments on fig 1B. Mutations added to fig 4D.; Altered as suggested; altered as suggested krit1_human Krev interaction trapped protein 1 KRIT1 CCM1 Cerebral cavernous malformations 1 protein protein protein human Homo sapiens Human MGNPENIEDAYVAVIRPKNTASLNSREYRAKSYEILLHEVPIEGQKKKRKKVLLETKLQGNSEITQGILDYVVETTKPISPANQGIRGKRVVLMKKFPLDGEKMGREASLFIVPSVVKDNTKYTYTPGCPIFYCLQDIMRVCSESSTHFATLTARMLIALDKWLDERHAQSHFIPALFRPSPLERIKTNVINPAYATESGQTENSLHMGYSALEIKSKMLALEKADTCIYNPLFGSDLQYTNRVDKVVINPYFGLGAPDYSKIQIPKQEKWQRSMSSVTEDKERQWVDDFPLHRSACEGDSELLSRLLSERFSVNQLDSDHWAPIHYACWYGKVEATRILLEKGKCNPNLLNGQLSSPLHFAAGGGHAEIVQILLNHPETDRHITDQQGRSPLNICEENKQNNWEEAAKLLKEAINKPYEKVRIYRMDGSYRSVELKHGNNTTVQQIMEGMRLSQETQQYFTIWICSENLSLQLKPYHKPLQHVRDWPEILAELTNLDPQRETPQLFLRRDVRLPLEVEKQIEDPLAILILFDEARYNLLKGFYTAPDAKLITLASLLLQIVYGNYESKKHKQGFLNEENLKSIVPVTKLKSKAPHWTNRILHEYKNLSTSEGVSKEMHHLQRMFLQNCWEIPTYGAAFFTGQIFTKASPSNHKVIPVYVGVNIKGLHLLNMETKALLISLKYGCFMWQLGDTDTCFQIHSMENKMSFIVHTKQAGLVVKLLMKLNGQLMPTERNS DIP protein O00522 original sequence version: 156 D11F75ED629E85AC heg1_human Protein HEG homolog 1 HEG1 KIAA1237 protein protein human Homo sapiens Human MASPRASRWPPPLLLLLLPLLLLPPAAPGTRDPPPSPARRALSLAPLAGAGLELQLERRPEREPPPTPPRERRGPATPGPSYRAPEPGAATQRGPSGRAPRGGSADAAWKHWPESNTEAHVENITFYQNQEDFSTVSSKEGVMVQTSGKSHAASDAPENLTLLAETADARGRSGSSSRTNFTILPVGYSLEIATALTSQSGNLASESLHLPSSSSEFDERIAAFQTKSGTASEMGTERAMGLSEEWTVHSQEATTSAWSPSFLPALEMGELTTPSRKRNSSGPDLSWLHFYRTAASSPLLDLSSSSESTEKLNNSTGLQSSSVSQTKTMHVATVFTDGGPRTLRSLTVSLGPVSKTEGFPKDSRIATTSSSVLLSPSAVESRRNSRVTGNPGDEEFIEPSTENEFGLTSLRWQNDSPTFGEHQLASSSEVQNGSPMSQTETVSRSVAPMRGGEITAHWLLTNSTTSADVTGSSASYPEGVNASVLTQFSDSTVQSGGSHTALGDRSYSESSSTSSSESLNSSAPRGERSIAGISYGQVRGTAIEQRTSSDHTDHTYLSSTFTKGERALLSITDNSSSSDIVESSTSYIKISNSSHSEYSSFFHAQTERSNISSYDGEYAQPSTESPVLHTSNLPSYTPTINMPNTSVVLDTDAEFVSDSSSSSSSSSSSSSSGPPLPLPSVSQSHHLFSSILPSTRASVHLLKSTSDASTPWSSSPSPLPVSLTTSTSAPLSVSQTTLPQSSSTPVLPRARETPVTSFQTSTMTSFMTMLHSSQTADLKSQSTPHQEKVITESKSPSLVSLPTESTKAVTTNSPLPPSLTESSTEQTLPATSTNLAQMSPTFTTTILKTSQPLMTTPGTLSSTASLVTGPIAVQTTAGKQLSLTHPEILVPQISTEGGISTERNRVIVDATTGLIPLTSVPTSAKEMTTKLGVTAEYSPASRSLGTSPSPQTTVVSTAEDLAPKSATFAVQSSTQSPTTVSSSASVNSCAVNPCLHNGECVADNTSRGYHCRCPPSWQGDDCSVDVNECLSNPCPSTAMCNNTQGSFICKCPVGYQLEKGICNLVRTFVTEFKLKRTFLNTTVEKHSDLQEVENEITKTLNMCFSALPSYIRSTVHASRESNAVVISLQTTFSLASNVTLFDLADRMQKCVNSCKSSAEVCQLLGSQRRIFRAGSLCKRKSPECDKDTSICTDLDGVALCQCKSGYFQFNKMDHSCRACEDGYRLENETCMSCPFGLGGLNCGNPYQLITVVIAAAGGGLLLILGIALIVTCCRKNKNDISKLIFKSGDFQMSPYAEYPKNPRSQEWGREAIEMHENGSTKNLLQMTDVYYSPTSVRNPELERNGLYPAYTGLPGSRHSCIFPGQYNPSFISDESRRRDYF 2E8402AC5227F95C ccm2_human Cerebral cavernous malformations 2 protein CCM2 C7orf22 Malcavernin PP10187 protein protein human Homo sapiens Human MEEEGKKGKKPGIVSPFKRVFLKGEKSRDKKAHEKVTERRPLHTVVLSLPERVEPDRLLSDYIEKEVKYLGQLTSIPGYLNPSSRTEILHFIDNAKRAHQLPGHLTQEHDAVLSLSAYNVKLAWRDGEDIILRVPIHDIAAVSYVRDDAAHLVVLKTAQDPGISPSQSLCAESSRGLSAGSLSESAVGPVEACCLVILAAESKVAAEELCCLLGQVFQVVYTESTIDFLDRAIFDGASTPTHHLSLHSDDSSTKVDIKETYEVEASTFCFPESVDVGGASPHSKTISESELSASATELLQDYMLTLRTKLSSQEIQQFAALLHEYRNGASIHEFCINLRQLYGDSRKFLLLGLRPFIPEKDSQHFENFLETIGVKDGRGIITDSFGRHRRALSTTSSSTTNGNRATGSSDDRSAPSEGDEWDRMISDISSDIEALGCSMDQDSA 43F9C153B4DE460E rap1a_mouse Ras-related protein Rap-1A Rap1a Krev-1 Ras-related protein Krev-1 protein protein mouse Mus musculus Mouse MREYKLVVLGSGGVGKSALTVQFVQGIFVEKYDPTIEDSYRKQVEVDCQQCMLEILDTAGTEQFTAMRDLYMKNGQGFALVYSITAQSTFNDLQDLREQILRVKDTEDVPMILVGNKCDLEDERVVGKEQGQNLARQWCNCAFLESSAKSKINVNEIFYDLVRQINRKTPVEKKKPKKKSCLLL 42C39290C98E0A92 krit1-heg1-1 4 8 unspecified role unspecified role bait bait n_terminus 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 ferm_domain sufficient to bind sufficient binding region sufficient to bind certain certain sequence position certain certain certain sequence position certain ecoli Escherichia coli (strain K12) 9 unspecified role unspecified role prey prey cytoplasmic_tail 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 ecoli Escherichia coli (strain K12) 15 17 physical association physical association 1A heg1-krit1-1 6 8 unspecified role unspecified role neutral component neutral component possible_tag tag tag undetermined undetermined sequence position undetermined undetermined undetermined sequence position undetermined ferm_domain sufficient to bind sufficient binding region sufficient to bind certain certain sequence position certain certain certain sequence position certain ecoli Escherichia coli (strain K12) 9 unspecified role unspecified role neutral component neutral component cytoplasmic_tail sufficient to bind sufficient binding region sufficient to bind 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 24 22 direct interaction direct interaction 1C heg1-krit1-2 7 8 unspecified role unspecified role neutral component neutral component ferm_domain sufficient to bind sufficient binding region sufficient to bind certain certain sequence position certain certain certain sequence position certain ecoli Escherichia coli (strain K12) 9 unspecified role unspecified role neutral component neutral component cytoplasmic_tail sufficient to bind sufficient binding region sufficient to bind certain certain sequence position certain certain certain sequence position certain direct interaction direct interaction Table 2 2.49A RWork =0.234 RFree =0.309 heg1-krit1-3 5 8 unspecified role unspecified role prey prey O00522:p.[Leu717Ala;Leu721Ala] mutation decreasing strength mutation decreasing interaction strength mutation decreasing strength certain certain sequence position certain certain certain sequence position certain L A certain certain sequence position certain certain certain sequence position certain L A Wed May 02 17:27:33 BST 2018 This feature has been corrected as a result of our quality control procedures. The original label was 'leu717ala,leu721ala' Tue Jun 30 18:09:28 BST 2020 This feature has been corrected as a result of our quality control procedures. The original label was 'p.[Leu717Ala;Leu721Ala]' n_terminus gfp tag green fluorescent protein tag GFP green fluorescent protein GFP green fluorescent protein gfp tag n-term range n-terminal range n-term range n-term range n-terminal range n-term range ferm_domain sufficient to bind sufficient binding region sufficient to bind certain certain sequence position certain certain certain sequence position certain 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. 9 unspecified role unspecified role bait bait cytoplasmic_tail sufficient to bind sufficient binding region sufficient to bind certain certain sequence position certain certain certain sequence position certain Q9ULI3:p.Tyr1380_Phe1381del mutation decreasing strength mutation decreasing interaction strength mutation decreasing strength certain certain sequence position certain certain certain sequence position certain YF .. Wed May 02 16:00:07 BST 2018 This feature has been corrected as a result of our quality control procedures. The original label was 'tyr_phe1380-1381del_del' Tue Jun 30 18:01:40 BST 2020 This feature has been corrected as a result of our quality control procedures. The original label was 'p.Tyr1380_Phe1381del' chemical synthesis Chemical synthesis (Chemical synthesis) physical association physical association 4 A/B heg1-krit1-4 2 8 unspecified role unspecified role bait bait O00522:p.[Leu717Ala;Leu721Ala] mutation with no effect mutation with no effect mutation with no effect mutation not affecting interaction certain certain sequence position certain certain certain sequence position certain L A certain certain sequence position certain certain certain sequence position certain L A Wed May 02 16:24:08 BST 2018 This feature has been corrected as a result of our quality control procedures. The original label was 'leu717ala,leu721ala' Tue Jun 30 18:42:38 BST 2020 This feature has been corrected as a result of our quality control procedures. The original label was 'p.[Leu717Ala;Leu721Ala]' n_terminus gfp tag green fluorescent protein tag GFP green fluorescent protein GFP green fluorescent protein gfp tag n-term range n-terminal range n-term range n-term range n-terminal range n-term range 10 unspecified role unspecified role prey prey n_terminus flag tag flag tag FLAG-tagged FLAG DYKDDDDKV epitope tag DYKDDDDKV epitope tag FLAG FLAG-tagged n-term range n-terminal range n-term range n-term range n-terminal range n-term range physical association physical association 4C krit1-rap1a-1 1 11 unspecified role unspecified role prey prey n_terminus ha tag ha tag YPYDVPDYA epitope tag YPYDVPDYA epitope tag n-term range n-terminal range n-term range n-term range n-terminal range n-term range P62835:p.Gly12Val mutation mutation certain certain sequence position certain certain certain sequence position certain G V Wed May 02 17:17:10 BST 2018 This feature has been corrected as a result of our quality control procedures. The original label was 'gly12val' Tue Jun 30 18:54:49 BST 2020 This feature has been corrected as a result of our quality control procedures. The original label was 'p.Gly12Val' 8 unspecified role unspecified role bait bait O00522:p.Arg452Glu mutation disrupting strength mutation disrupting interaction strength mutation disrupting strength certain certain sequence position certain certain certain sequence position certain R E Wed May 02 17:31:18 BST 2018 This feature has been corrected as a result of our quality control procedures. The original label was 'arg452glu' Tue Jun 30 17:43:50 BST 2020 This feature has been corrected as a result of our quality control procedures. The original label was 'p.Arg452Glu' n_terminus 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 O00522:p.[Leu717Ala;Leu721Ala] mutation with no effect mutation with no effect mutation with no effect mutation not affecting interaction certain certain sequence position certain certain certain sequence position certain L A certain certain sequence position certain certain certain sequence position certain L A Wed May 02 20:05:21 BST 2018 This feature has been corrected as a result of our quality control procedures. The original label was 'leu717ala,leu721ala' Tue Jun 30 16:09:23 BST 2020 This feature has been corrected as a result of our quality control procedures. The original label was 'p.[Leu717Ala;Leu721Ala]' ferm_domain 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 4D heg1-krit1-5 3 8 unspecified role unspecified role bait bait n_terminus gfp tag green fluorescent protein tag GFP green fluorescent protein GFP green fluorescent protein gfp tag n-term range n-terminal range n-term range n-term range n-terminal range n-term range ferm_domain sufficient to bind sufficient binding region sufficient to bind certain certain sequence position certain certain certain sequence position certain 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. 9 unspecified role unspecified role prey prey cytoplasmic_tail sufficient to bind sufficient binding region sufficient to bind certain certain sequence position certain certain certain sequence position certain cytoplasmic_tail binding region binding-associated region binding region certain certain sequence position certain certain certain sequence position certain Q9ULI3:p.[Asn1367Ala;Phe1370Ala] mutation with no effect mutation with no effect mutation with no effect mutation not affecting interaction certain certain sequence position certain certain certain sequence position certain N A certain certain sequence position certain certain certain sequence position certain F A Wed May 02 18:22:14 BST 2018 This feature has been corrected as a result of our quality control procedures. The original label was 'asn1367ala,phe1370ala' Tue Jun 30 19:03:28 BST 2020 This feature has been corrected as a result of our quality control procedures. The original label was 'p.[Asn1367Ala;Phe1370Ala]' 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 ecoli Escherichia coli (strain K12) 59 57 physical association physical association 1B