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/ Functional interactions between FOXC1 and PITX2 underlie the sensitivity to FOXC1 gene dose in Axenfeld-Rieger syndrome and anterior segment dysgenesis. Functional interactions between FOXC1 and PITX2 underlie the sensitivity to FOXC1 gene dose in Axenfeld-Rieger syndrome and anterior segment dysgenesis. Hum. Mol. Genet. (0964-6906) 2006 imex curation Berry FB., Lines MA., Oas JM., Footz T., Underhill DA., Gage PJ., Walter MA. Deparaffinized, paraffin embeded transverse sections of whole eye primordia from E11.5, E12.5 and E16.5 were coimmunostained. fberry@ualberta.ca 21-Dec-2006: Contacted by JYOTI. Only protein-protein interactions mouse-embryo Mus musculus embryo embryo Embryo Defined as the development stage prior to the initiation of tissue differentiation. confocal microscopy confocal microscopy immunostaining immunostaining Berry FB., Lines MA., Oas JM., Footz T., Underhill DA., Gage PJ., Walter MA. Deparaffinized, paraffin embeded transverse sections of whole eye primordia from E11.5, E12.5 and E16.5 were coimmunostained. fberry@ualberta.ca Accepted 2006-DEC-11 by JYOTI. Deparaffinized, paraffin embeded transverse sections of whole eye primordia from E11.5, E12.5 and E16.5 were coimmunostained. 21-Dec-2006: Contacted by JYOTI. Hum. Mol. Genet. (0964-6906) 2006 Only protein-protein interactions imex curation Functional interactions between FOXC1 and PITX2 underlie the sensitivity to FOXC1 gene dose in Axenfeld-Rieger syndrome and anterior segment dysgenesis. Functional interactions between FOXC1 and PITX2 underlie the sensitivity to FOXC1 gene dose in Axenfeld-Rieger syndrome and anterior segment dysgenesis. Hum. Mol. Genet. (0964-6906) 2006 imex curation Berry FB., Lines MA., Oas JM., Footz T., Underhill DA., Gage PJ., Walter MA. Deparaffinized, paraffin embeded transverse sections of whole eye primordia from E11.5, E12.5 and E16.5 were coimmunostained. fberry@ualberta.ca 21-Dec-2006: Contacted by JYOTI. Only protein-protein interactions chlae-cos_7 Cercopithecus aethiops simian cells transformed with SV40 Grivet cos_7 cercopithecus aethiops, by transformation with SV40 confocal microscopy confocal microscopy immunostaining immunostaining Berry FB., Lines MA., Oas JM., Footz T., Underhill DA., Gage PJ., Walter MA. Deparaffinized, paraffin embeded transverse sections of whole eye primordia from E11.5, E12.5 and E16.5 were coimmunostained. fberry@ualberta.ca Accepted 2006-DEC-11 by JYOTI. Deparaffinized, paraffin embeded transverse sections of whole eye primordia from E11.5, E12.5 and E16.5 were coimmunostained. 21-Dec-2006: Contacted by JYOTI. Hum. Mol. Genet. (0964-6906) 2006 Only protein-protein interactions imex curation Functional interactions between FOXC1 and PITX2 underlie the sensitivity to FOXC1 gene dose in Axenfeld-Rieger syndrome and anterior segment dysgenesis. Functional interactions between FOXC1 and PITX2 underlie the sensitivity to FOXC1 gene dose in Axenfeld-Rieger syndrome and anterior segment dysgenesis. Hum. Mol. Genet. (0964-6906) 2006 imex curation Berry FB., Lines MA., Oas JM., Footz T., Underhill DA., Gage PJ., Walter MA. Deparaffinized, paraffin embeded transverse sections of whole eye primordia from E11.5, E12.5 and E16.5 were coimmunostained. fberry@ualberta.ca 21-Dec-2006: Contacted by JYOTI. Only protein-protein interactions chlae-cos_7 Cercopithecus aethiops simian cells transformed with SV40 Grivet cos_7 cercopithecus aethiops, by transformation with SV40 anti tag coip anti tag coimmunoprecipitation anti tag coip western blot western blot Immuno blot Immuno blot Berry FB., Lines MA., Oas JM., Footz T., Underhill DA., Gage PJ., Walter MA. Deparaffinized, paraffin embeded transverse sections of whole eye primordia from E11.5, E12.5 and E16.5 were coimmunostained. fberry@ualberta.ca Accepted 2006-DEC-11 by JYOTI. Deparaffinized, paraffin embeded transverse sections of whole eye primordia from E11.5, E12.5 and E16.5 were coimmunostained. 21-Dec-2006: Contacted by JYOTI. Hum. Mol. Genet. (0964-6906) 2006 Only protein-protein interactions imex curation Functional interactions between FOXC1 and PITX2 underlie the sensitivity to FOXC1 gene dose in Axenfeld-Rieger syndrome and anterior segment dysgenesis. Functional interactions between FOXC1 and PITX2 underlie the sensitivity to FOXC1 gene dose in Axenfeld-Rieger syndrome and anterior segment dysgenesis. Hum. Mol. Genet. (0964-6906) 2006 imex curation Berry FB., Lines MA., Oas JM., Footz T., Underhill DA., Gage PJ., Walter MA. Deparaffinized, paraffin embeded transverse sections of whole eye primordia from E11.5, E12.5 and E16.5 were coimmunostained. fberry@ualberta.ca 21-Dec-2006: Contacted by JYOTI. Only protein-protein interactions chlae-cos_7 Cercopithecus aethiops simian cells transformed with SV40 Grivet cos_7 cercopithecus aethiops, by transformation with SV40 pull down pull down western blot western blot Immuno blot Immuno blot Berry FB., Lines MA., Oas JM., Footz T., Underhill DA., Gage PJ., Walter MA. Deparaffinized, paraffin embeded transverse sections of whole eye primordia from E11.5, E12.5 and E16.5 were coimmunostained. fberry@ualberta.ca Accepted 2006-DEC-11 by JYOTI. Deparaffinized, paraffin embeded transverse sections of whole eye primordia from E11.5, E12.5 and E16.5 were coimmunostained. 21-Dec-2006: Contacted by JYOTI. Hum. Mol. Genet. (0964-6906) 2006 Only protein-protein interactions imex curation foxc1_mouse Forkhead box protein C1 Forkhead-related protein FKHL7 Forkhead-related transcription factor 3 Transcription factor FKH-1 Mesoderm/mesenchyme forkhead 1 Foxc1 Fkh1 Fkhl7 Freac3 Mf1 protein protein mouse Mus musculus Mouse MQARYSVSSPNSLGVVPYLGGEQSYYRAAAAAAGGGYTAMPAPMSVYSHPAHAEQYPGSMARAYGPYTPQPQPKDMVKPPYSYIALITMAIQNAPDKKITLNGIYQFIMDRFPFYRDNKQGWQNSIRHNLSLNECFVKVPRDDKKPGKGSYWTLDPDSYNMFENGSFLRRRRRFKKKDAVKDKEEKGRLHLQEPPPPQAGRQPAPAPPEQAEGSAPGPQPPPVRIQDIKTENGTCPSPPQPLSPAAALGSGSAATVPKIESPDSSSSSLSSGSSPPGSLPSARPLSLDAAEPAPPPQPAPPPHHSQGFSVDNIMTSLRGSPQGSAAELGSGLLASAAASSRAGIAPPLALGAYSPGQSSLYSSPCSQSSSAGSSGGGGGGGGGGGGSSSAAGTGGAATYHCNLQAMSLYAAGERGGHLQGPAGGAGSAAVDDPLPDYSLPPATSSSSSSLSHGGGGQEASHHPASHQGRLTSWYLNQAGGDLGHLASAAAAAAAAGYPGQQQNFHSVREMFESQRIGLNNSPVNGNSSCQMAFPASQSLYRTSGAFVYDCSKF 3CDB14F69AA2F217 q99697-3 Pituitary homeobox 2 ARP1A PITX2 ARP1 RGS RIEG RIEG1 ALL1-responsive protein ARP1 Homeobox protein PITX2 Paired-like homeodomain transcription factor 2 RIEG bicoid-related homeobox transcription factor Solurshin protein protein human Homo sapiens Human METNCRKLVSACVQLEKDKSQQGKNEDVGAEDPSKKKRQRRQRTHFTSQQLQELEATFQRNRYPDMSTREEIAVWTNLTEARVRVWFKNRRAKWRKRERNQQAELCKNGFGPQFNGLMQPYDDMYPGYSYNNWAAKGLTSASLSTKSFPFFNSMNVNPLSSQSMFSPPNSISSMSMSSSMVPSAVTGVPGSSLNSLNNLNNLSSPSLNSAVPTPACPYAPPTPPYVYRDTCNSSLASLRLKAKQHSSFGYASVQNPASNLSACQYAVDRPV Variant in position: 58:F->L (in ASGD4). 45D2ADA6DF03FF65 pitx2_mouse Pituitary homeobox 2 BRX1 homeoprotein Paired-like homeodomain transcription factor Munc 30 Pitx2 Arp1 Brx1 Otlx2 Ptx2 Rgs Orthodenticle-like homeobox 2 Solurshin ALL1-responsive protein ARP1 Paired-like homeodomain transcription factor 2 Homeobox protein PITX2 protein protein mouse Mus musculus Mouse METNCRKLVSACVQLGVQPAAVECLFSKDSEIKKVEFTDSPKSRKESASSKLFPRQHPGANEKDKGQQGKNEDVGAEDPSKKKRQRRQRTHFTSQQLQELEATFQRNRYPDMSTREEIAVWTNLTEARVRVWFKNRRAKWRKRERNQQAELCKNGFGPQFNGLMQPYDDMYPGYSYNNWAAKGLTSASLSTKSFPFFNSMNVNPLSSQSMFSPPNSISSMSMSSSMVPSAVTGVPGSSLNSLNNLNNLSSPSLNSAVPTPACPYAPPTPPYVYRDTCNSSLASLRLKAKQHSSFGYASVQNPASNLSACQYAVDRPV DIP protein P97474 original sequence version: 151 188315708E6BD95D foxc1_human Forkhead box protein C1 Forkhead-related protein FKHL7 Forkhead-related transcription factor 3 FOXC1 FKHL7 FREAC3 protein protein human Homo sapiens Human MQARYSVSSPNSLGVVPYLGGEQSYYRAAAAAAGGGYTAMPAPMSVYSHPAHAEQYPGGMARAYGPYTPQPQPKDMVKPPYSYIALITMAIQNAPDKKITLNGIYQFIMDRFPFYRDNKQGWQNSIRHNLSLNECFVKVPRDDKKPGKGSYWTLDPDSYNMFENGSFLRRRRRFKKKDAVKDKEEKDRLHLKEPPPPGRQPPPAPPEQADGNAPGPQPPPVRIQDIKTENGTCPSPPQPLSPAAALGSGSAAAVPKIESPDSSSSSLSSGSSPPGSLPSARPLSLDGADSAPPPPAPSAPPPHHSQGFSVDNIMTSLRGSPQSAAAELSSGLLASAAASSRAGIAPPLALGAYSPGQSSLYSSPCSQTSSAGSSGGGGGGAGAAGGAGGAGTYHCNLQAMSLYAAGERGGHLQGAPGGAGGSAVDDPLPDYSLPPVTSSSSSSLSHGGGGGGGGGGQEAGHHPAAHQGRLTSWYLNQAGGDLGHLASAAAAAAAAGYPGQQQNFHSVREMFESQRIGLNNSPVNGNSSCQMAFPSSQSLYRTSGAFVYDCSKF 59C6FB94303ED59A pitx2-foxc1-1 1 5 unspecified role unspecified role neutral component neutral component 7 unspecified role unspecified role neutral component neutral component colocalization colocalization 1 PITX2 and FOXC1 colocalize in the developing mouse eye pitx2a-foxc1-2 3 8 unspecified role unspecified role prey prey xpress tag tag tag undetermined undetermined sequence position undetermined undetermined undetermined sequence position undetermined 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 bait bait region 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 physical association physical association 2A and 3 Xp-FOXC1 was recovered in {alpha}-HA IP isolates in an HA-PITX2A-dependent fashion foxc1-pitx2a-1 3 6 unspecified role unspecified role prey prey region 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 8 unspecified role unspecified role bait bait xpress tag tag tag undetermined undetermined sequence position undetermined undetermined undetermined sequence position undetermined physical association physical association 2B HA-PITX2A was recovered by {alpha}-Xpress in an Xp-FOXC1-dependent manner foxc1-pitx2a-2 4 6 unspecified role unspecified role prey prey region 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 region required to bind necessary binding region required to bind certain certain sequence position certain certain certain sequence position certain region required to bind necessary binding region required to bind certain certain sequence position certain certain certain sequence position certain region required to bind necessary binding region required to bind certain certain sequence position certain certain certain sequence position certain 8 unspecified role unspecified role bait bait 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) physical association physical association 4A Full-length PITX2A bound to Ni2+-FOXC1 in these assays pitx2a-foxc1-3 4 8 unspecified role unspecified role prey prey region v5 tag v5 tag GKPIPNPLLGLDST epitope tag GKPIPNPLLGLDST epitope tag undetermined undetermined sequence position undetermined undetermined undetermined sequence position undetermined 6 unspecified role unspecified role bait bait region 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 region required to bind necessary binding region required to bind certain certain sequence position certain certain certain sequence position certain ecoli Escherichia coli (strain K12) physical association physical association 4B deletion of the PITX2A HD ({Delta}39-98) ablated FOXC1 interactions. foxc1-pitx2a-3 2 6 unspecified role unspecified role neutral component neutral component xpress tag tag tag undetermined undetermined sequence position undetermined undetermined undetermined sequence position undetermined Q99697-3:p.Thr68Pro mutation decreasing mutation decreasing interaction hotspot hotspot mutation decreasing mutation analysis mutation analysis certain certain sequence position certain certain certain sequence position certain T P Wed May 02 16:14:53 BST 2018 This feature has been corrected as a result of our quality control procedures. The original label was 'thr68pro' Tue Jun 30 16:56:58 BST 2020 This feature has been corrected as a result of our quality control procedures. The original label was 'p.Thr68Pro' Q99697-3:p.Arg91Pro mutation decreasing mutation decreasing interaction hotspot hotspot mutation decreasing mutation analysis mutation analysis certain certain sequence position certain certain certain sequence position certain R P Wed May 02 17:28:52 BST 2018 This feature has been corrected as a result of our quality control procedures. The original label was 'arg91pro' Tue Jun 30 15:37:14 BST 2020 This feature has been corrected as a result of our quality control procedures. The original label was 'p.Arg91Pro' Q99697-3:p.Lys88Glu mutation decreasing mutation decreasing interaction hotspot hotspot mutation decreasing mutation analysis mutation analysis certain certain sequence position certain certain certain sequence position certain K E Wed May 02 19:30:45 BST 2018 This feature has been corrected as a result of our quality control procedures. The original label was 'lys88glu' Tue Jun 30 18:57:19 BST 2020 This feature has been corrected as a result of our quality control procedures. The original label was 'p.Lys88Glu' 8 unspecified role unspecified role neutral component neutral component region gfp tag green fluorescent protein tag GFP green fluorescent protein GFP green fluorescent protein gfp tag undetermined undetermined sequence position undetermined undetermined undetermined sequence position undetermined colocalization colocalization 6 FOXC1-GFP and WT PITX2A were indeed highly colocalized within the cell nucleus Colocalisation to Hoechst stained chromatin but exclusion from the densest part of Hoechst foci observed. pitx2a-foxc1-4 2 8 unspecified role unspecified role neutral component neutral component region gfp tag green fluorescent protein tag GFP green fluorescent protein GFP green fluorescent protein gfp tag undetermined undetermined sequence position undetermined undetermined undetermined sequence position undetermined Q12948:p.Ser131Leu mutation decreasing strength mutation decreasing interaction strength mutation decreasing strength certain certain sequence position certain certain certain sequence position certain S L Wed May 02 18:14:59 BST 2018 This feature has been corrected as a result of our quality control procedures. The original label was 'ser131leu' Tue Jun 30 16:01:07 BST 2020 This feature has been corrected as a result of our quality control procedures. The original label was 'p.Ser131Leu' Q12948:p.Arg127His mutation decreasing strength mutation decreasing interaction strength mutation decreasing strength certain certain sequence position certain certain certain sequence position certain R H Wed May 02 18:55:58 BST 2018 This feature has been corrected as a result of our quality control procedures. The original label was 'arg127his' Tue Jun 30 16:13:19 BST 2020 This feature has been corrected as a result of our quality control procedures. The original label was 'p.Arg127His' 6 unspecified role unspecified role neutral component neutral component region 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 colocalization colocalization 8 colocalization between HA-PITX2A and R127H or S131L FOXC1-GFP is largely disrupted.