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/ Ectodermal factor restricts mesoderm differentiation by inhibiting p53. Ectodermal factor restricts mesoderm differentiation by inhibiting p53. Cell (0092-8674) 2008 imex curation Sasai N., Yakura R., Kamiya D., Nakazawa Y., Sasai Y. Apoptosis - Interactions involving proteins with a function related to apoptosis norisa@cdb.riken.jp 27-Aug-2008: Contacted by JYOTI. orchard Only protein-protein interactions 4 xenla-animal_cap Xenopus laevis animal cap animal_cap Animal cap Xenopus laevis animal cap cells are cells situated around the animal (pigmented) pole of a blastula or very early gastrula-stage embryo. This tissue is fated to become cement gland/neurectoderm on the dorsal side of the embryo and epidermis on the ventral side. Animal caps are composed of pluripotent cells that can be induced to form endodermal, mesodermal, or ectodermal cell types. XAO:0000036. ch-ip chromatin immunoprecipitation assay ch-ip primer specific pcr primer specific pcr Sasai N., Yakura R., Kamiya D., Nakazawa Y., Sasai Y. Apoptosis - Interactions involving proteins with a function related to apoptosis norisa@cdb.riken.jp Accepted 2008-AUG-9 by ORCHARD. 27-Aug-2008: Contacted by JYOTI. Cell (0092-8674) 2008 orchard Only protein-protein interactions 4 imex curation Ectodermal factor restricts mesoderm differentiation by inhibiting p53. Ectodermal factor restricts mesoderm differentiation by inhibiting p53. Cell (0092-8674) 2008 imex curation Sasai N., Yakura R., Kamiya D., Nakazawa Y., Sasai Y. Apoptosis - Interactions involving proteins with a function related to apoptosis norisa@cdb.riken.jp 27-Aug-2008: Contacted by JYOTI. orchard Only protein-protein interactions 4 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 anti tag western anti tag western blot anti tag western Sasai N., Yakura R., Kamiya D., Nakazawa Y., Sasai Y. Apoptosis - Interactions involving proteins with a function related to apoptosis norisa@cdb.riken.jp Accepted 2008-AUG-9 by ORCHARD. Cell (0092-8674) 2008 orchard Only protein-protein interactions 4 imex curation Ectodermal factor restricts mesoderm differentiation by inhibiting p53. Ectodermal factor restricts mesoderm differentiation by inhibiting p53. Cell (0092-8674) 2008 imex curation Sasai N., Yakura R., Kamiya D., Nakazawa Y., Sasai Y. Apoptosis - Interactions involving proteins with a function related to apoptosis norisa@cdb.riken.jp 27-Aug-2008: Contacted by JYOTI. orchard Only protein-protein interactions 4 xenla-animal_cap Xenopus laevis animal cap animal_cap Animal cap Xenopus laevis animal cap cells are cells situated around the animal (pigmented) pole of a blastula or very early gastrula-stage embryo. This tissue is fated to become cement gland/neurectoderm on the dorsal side of the embryo and epidermis on the ventral side. Animal caps are composed of pluripotent cells that can be induced to form endodermal, mesodermal, or ectodermal cell types. XAO:0000036. anti tag coip anti tag coimmunoprecipitation anti tag coip western blot western blot Immuno blot Immuno blot Sasai N., Yakura R., Kamiya D., Nakazawa Y., Sasai Y. Apoptosis - Interactions involving proteins with a function related to apoptosis norisa@cdb.riken.jp Accepted 2008-AUG-9 by ORCHARD. 27-Aug-2008: Contacted by JYOTI. Cell (0092-8674) 2008 orchard Only protein-protein interactions 4 imex curation Ectodermal factor restricts mesoderm differentiation by inhibiting p53. Ectodermal factor restricts mesoderm differentiation by inhibiting p53. Cell (0092-8674) 2008 imex curation Sasai N., Yakura R., Kamiya D., Nakazawa Y., Sasai Y. Apoptosis - Interactions involving proteins with a function related to apoptosis norisa@cdb.riken.jp 27-Aug-2008: Contacted by JYOTI. orchard Only protein-protein interactions 4 in vitro In vitro pull down pull down weight autoradiogra molecular weight estimation by autoradiography weight autoradiogra Sasai N., Yakura R., Kamiya D., Nakazawa Y., Sasai Y. Apoptosis - Interactions involving proteins with a function related to apoptosis norisa@cdb.riken.jp Accepted 2008-AUG-9 by ORCHARD. 27-Aug-2008: Contacted by JYOTI. Cell (0092-8674) 2008 orchard Only protein-protein interactions 4 imex curation Ectodermal factor restricts mesoderm differentiation by inhibiting p53. Ectodermal factor restricts mesoderm differentiation by inhibiting p53. Cell (0092-8674) 2008 imex curation Sasai N., Yakura R., Kamiya D., Nakazawa Y., Sasai Y. Apoptosis - Interactions involving proteins with a function related to apoptosis norisa@cdb.riken.jp 27-Aug-2008: Contacted by JYOTI. orchard Only protein-protein interactions 4 in vitro In vitro emsa supershift electrophoretic mobility supershift assay emsa supershift anti tag western anti tag western blot anti tag western Sasai N., Yakura R., Kamiya D., Nakazawa Y., Sasai Y. Apoptosis - Interactions involving proteins with a function related to apoptosis norisa@cdb.riken.jp Accepted 2008-AUG-9 by ORCHARD. 27-Aug-2008: Contacted by JYOTI. Cell (0092-8674) 2008 orchard Only protein-protein interactions 4 imex curation mix_2_xenla_gene Xenopus laevis Mix.2 promoter DNA sequence gene gene xenla Xenopus laevis (African clawed frog) African clawed frog p53_xenla Cellular tumor antigen p53 Tumor suppressor p53 tp53 protein protein xenla Xenopus laevis (African clawed frog) African clawed frog MEPSSETGMDPPLSQETFEDLWSLLPDPLQTVTCRLDNLSEFPDYPLAADMTVLQEGLMGNAVPTVTSCAVPSTDDYAGKYGLQLDFQQNGTAKSVTCTYSPELNKLFCQLAKTCPLLVRVESPPPRGSILRATAVYKKSEHVAEVVKRCPHHERSVEPGEDAAPPSHLMRVEGNLQAYYMEDVNSGRHSVCVPYEGPQVGTECTTVLYNYMCNSSCMGGMNRRPILTIITLETPQGLLLGRRCFEVRVCACPGRDRRTEEDNYTKKRGLKPSGKRELAHPPSSEPPLPKKRLVVVDDDEEIFTLRIKGRSRYEMIKKLNDALELQESLDQQKVTIKCRKCRDEIKPKKGKKLLVKDEQPDSE CE1F3E58F020D74D p53_be_human_dna Human p53 Binding Element DNA oligonucleotide ds dna double stranded deoxyribonucleic acid ds DNA ds dna human Homo sapiens Human TTTAGTCCTGTAGGCCAGGTCTGAGCCTGCACATCCCAGACAAG 4C8B48F36B6BA486 p53_human Cellular tumor antigen p53 TP53 P53 Tumor suppressor p53 Phosphoprotein p53 Antigen NY-CO-13 protein protein human Homo sapiens Human MEEPQSDPSVEPPLSQETFSDLWKLLPENNVLSPLPSQAMDDLMLSPDDIEQWFTEDPGPDEAPRMPEAAPPVAPAPAAPTPAAPAPAPSWPLSSSVPSQKTYQGSYGFRLGFLHSGTAKSVTCTYSPALNKMFCQLAKTCPVQLWVDSTPPPGTRVRAMAIYKQSQHMTEVVRRCPHHERCSDSDGLAPPQHLIRVEGNLRVEYLDDRNTFRHSVVVPYEPPEVGSDCTTIHYNYMCNSSCMGGMNRRPILTIITLEDSSGNLLGRNSFEVRVCACPGRDRRTEEENLRKKGEPHHELPPGSTKRALPNNTSSSPQPKKKPLDGEYFTLQIRGRERFEMFRELNEALELKDAQAGKEPGGSRAHSSHLKSKKGQSTSRHKKLMFKTEGPDSD DIP protein P04637 original sequence version: 121 DIP protein P04637 original sequence version: 115 DIP protein P04637-1 original sequence version: 224 DIP protein P04637 original sequence version: 117 DIP protein P04637-1 original sequence version: 226 DIP protein P04637 original sequence version: 226 DIP protein P04637 original sequence version: 212 DIP protein P04637 original sequence version: 220 DIP protein P04637-1 original sequence version: 220 DIP protein P04637-1 original sequence version: 145 DIP protein P04637 original sequence version: 146 DIP protein P04637 original sequence version: 145 DIP protein P04637 original sequence version: 166 DIP protein P04637-1 original sequence version: 166 DIP protein P04637 original sequence version: 169 DIP protein P04637 original sequence version: 177 DIP protein P04637 original sequence version: 175 DIP protein P04637-1 original sequence version: 175 DIP protein P04637-1 original sequence version: 172 DIP protein P04637-1 original sequence version: 169 DIP protein P04637 original sequence version: 170 DIP protein P04637 original sequence version: 172 DIP protein P04637-1 original sequence version: 194 DIP protein P04637 original sequence version: 196 DIP protein P04637 original sequence version: 185 DIP protein P04637-1 original sequence version: 191 DIP protein P04637 original sequence version: 191 DIP protein P04637 original sequence version: 180 DIP protein P04637-1 original sequence version: 197 DIP protein P04637 original sequence version: 183 DIP protein P04637-1 original sequence version: 183 DIP protein P04637-1 original sequence version: 185 DIP protein P04637 original sequence version: 199 DIP protein P04637 original sequence version: 201 DIP protein P04637 original sequence version: 189 DIP protein P04637 original sequence version: 235 DIP protein P04637 original sequence version: 230 DIP protein P04637 original sequence version: 234 DIP protein P04637-1 original sequence version: 234 DIP protein P04637-1 original sequence version: 235 DIP protein P04637 original sequence version: 239 DIP protein P04637-1 original sequence version: 212 DIP protein P04637-1 original sequence version: 213 DIP protein P04637 original sequence version: 213 DIP protein P04637 original sequence version: 206 DIP protein P04637-1 original sequence version: 188 DIP protein P04637-1 original sequence version: 228 DIP protein P04637 original sequence version: 208 DIP protein P04637 original sequence version: 240 DIP protein P04637-1 original sequence version: 240 DIP protein P04637 original sequence version: 204 DIP protein P04637-1 original sequence version: 204 DIP protein P04637-1 original sequence version: 209 DIP protein P04637-1 original sequence version: 203 DIP protein P04637 original sequence version: 221 DIP protein P04637-1 original sequence version: 152 DIP protein P04637 original sequence version: 217 DIP protein P04637-1 original sequence version: 140 DIP protein P04637 original sequence version: 215 DIP protein P04637 original sequence version: 214 DIP protein P04637-1 original sequence version: 182 DIP protein P04637 original sequence version: 182 DIP protein P04637 original sequence version: 188 DIP protein P04637 original sequence version: 192 DIP protein P04637-1 original sequence version: 192 DIP protein P04637 original sequence version: 218 DIP protein P04637-1 original sequence version: 218 AD5C149FD8106131 q9pst7_xenla znf585b.S znf585b protein protein xenla Xenopus laevis (African clawed frog) African clawed frog MMHLIRNWPEKEKQNLNGSEMSRMKKIIEVGSERENIWGNLSQTQTHKESYRTPNQNYTSPMPQEYSYNGKLFALQREKLHNTNVQVIRMPNIAKQPKFNREIRSDSPKRKKAKSSEKSHVANISHQGTKINKFSKAQSALKSFICPICKRRFCNARNLLTHQRIHTGRRFVCSKCGKCFSNKKILIAHRWLHTGRKPFTCTKCNKGFLWNRDLQKHEKSHKEMRNKSLGLVHRHDKLREVSTDPCKREKSFDCTECGKSFKRKSKLKTHFLCHTGEKPFVCVHCGKGFRDNYKLSLHLRIHTGENLSVCPDCGKSYTDKNKLIVHMRIHTGEKFMCSECGKGFSDFYNLKSHLQIHTGEKPFVCPECGKSFLSKYEFKSHLLIHTGKYPFICSECGKSFMDKRYLKIHSNVHSGNTFPCTECGKSFAAKQNLKRHQKIHTGEKPHKCTECGKQFLQKNKLDRHHLSHTGVKPFSCFECGEQFTWKHLLQYHQLSHTGERPFVCSECGKGYKTKASLALHCHIHTGEKPFVCPECGNSYRSNGALRYHLQTHIKGKYFAHSEHGESDKSETNE 9363D3B0CC429D2D tp53-xfdl 2 10 unspecified role unspecified role prey prey region flag tag flag tag FLAG-tagged FLAG DYKDDDDKV epitope tag DYKDDDDKV epitope tag FLAG FLAG-tagged undetermined undetermined sequence position undetermined undetermined undetermined sequence position undetermined 9 unspecified role unspecified role bait bait region ha tag ha tag YPYDVPDYA epitope tag YPYDVPDYA epitope tag undetermined undetermined sequence position undetermined undetermined undetermined sequence position undetermined P04637:p.[Lys370Gln;Lys372Gln;Lys373Gln;Lys381Gln;Lys382Gln] mutation decreasing mutation decreasing interaction hotspot hotspot mutation decreasing mutation analysis mutation analysis certain certain sequence position certain certain certain sequence position certain K Q certain certain sequence position certain certain certain sequence position certain K Q certain certain sequence position certain certain certain sequence position certain K Q certain certain sequence position certain certain certain sequence position certain K Q certain certain sequence position certain certain certain sequence position certain K Q Wed May 02 15:59:38 BST 2018 This feature has been corrected as a result of our quality control procedures. The original label was 'lys370gln,lys372gln,lys373gln,lys381gln,lys382gln' Tue Jun 30 17:56:15 BST 2020 This feature has been corrected as a result of our quality control procedures. The original label was 'p.[Lys370Gln;Lys372Gln;Lys373Gln;Lys381Gln;Lys382Gln]' P04637:p.[Lys370Arg;Lys372Arg;Lys373Arg;Lys381Arg;Lys382Arg] mutation increasing mutation increasing interaction mutation increasing mutation analysis mutation analysis certain certain sequence position certain certain certain sequence position certain K R certain certain sequence position certain certain certain sequence position certain K R certain certain sequence position certain certain certain sequence position certain K R certain certain sequence position certain certain certain sequence position certain K R certain certain sequence position certain certain certain sequence position certain K R Wed May 02 18:30:16 BST 2018 This feature has been corrected as a result of our quality control procedures. The original label was 'lys370arg,lys372arg,lys373arg,lys381arg,lys382arg' Tue Jun 30 16:20:33 BST 2020 This feature has been corrected as a result of our quality control procedures. The original label was 'p.[Lys370Arg;Lys372Arg;Lys373Arg;Lys381Arg;Lys382Arg]' P04637:p.[Lys373Arg;Lys382Arg] mutation increasing mutation increasing interaction mutation increasing mutation analysis mutation analysis certain certain sequence position certain certain certain sequence position certain K R certain certain sequence position certain certain certain sequence position certain K R Wed May 02 17:51:55 BST 2018 This feature has been corrected as a result of our quality control procedures. The original label was 'lys373arg,lys382arg' Tue Jun 30 16:09:42 BST 2020 This feature has been corrected as a result of our quality control procedures. The original label was 'p.[Lys373Arg;Lys382Arg]' P04637:p.[Lys373Gln;Lys382Gln] mutation decreasing mutation decreasing interaction hotspot hotspot mutation decreasing mutation analysis mutation analysis certain certain sequence position certain certain certain sequence position certain K Q certain certain sequence position certain certain certain sequence position certain K Q Wed May 02 19:41:52 BST 2018 This feature has been corrected as a result of our quality control procedures. The original label was 'lys373gln,lys382gln' Tue Jun 30 20:19:00 BST 2020 This feature has been corrected as a result of our quality control procedures. The original label was 'p.[Lys373Gln;Lys382Gln]' n-terminal hp53DeltaRD sufficient to bind sufficient binding region sufficient to bind deletion analysis deletion analysis certain certain sequence position certain certain certain sequence position certain physical association physical association 5 A, 6 A, 6 G, S4 D Immunoprecipitation analysis using HEK293 lysates (Figure 5A) showed that XFDL efficiently coprecipitated with p53 (lane 4; human). P04637; Q9PST7 transfection tp53-xfdl-1 3 10 unspecified role unspecified role prey prey 7 unspecified role unspecified role bait bait region ha tag ha tag YPYDVPDYA epitope tag YPYDVPDYA epitope tag undetermined undetermined sequence position undetermined undetermined undetermined sequence position undetermined physical association physical association 5 B immunoprecipitation of endogenous XFDL protein with HA-tagged Xenopus p53 was seen from animal cap extracts P07193 injection tp53-xfdl-2 4 9 unspecified role unspecified role bait bait 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 10 unspecified role unspecified role prey prey region 35s radiolabel 35s radiolabel 35S s35 radiolabelled S35 s35 radiolabelled 35S S35 undetermined undetermined sequence position undetermined undetermined undetermined sequence position undetermined in vitro In vitro direct interaction direct interaction 5 C a strong physical association was seen between in vitro-translated XFDL protein and recombinant GST-hp53 protein, indicating that the two proteins directly interact It was not possible to determine what cell type was used to express the GST-tp53. p53_be_human-tp53 5 9 unspecified role unspecified role prey prey region ha tag ha tag YPYDVPDYA epitope tag YPYDVPDYA epitope tag undetermined undetermined sequence position undetermined undetermined undetermined sequence position undetermined P04637:p.[Lys373Gln;Lys382Gln] mutation increasing mutation increasing interaction mutation increasing mutation analysis mutation analysis certain certain sequence position certain certain certain sequence position certain K Q certain certain sequence position certain certain certain sequence position certain K Q Wed May 02 19:39:29 BST 2018 This feature has been corrected as a result of our quality control procedures. The original label was 'lys373gln,lys382gln' Tue Jun 30 18:50:16 BST 2020 This feature has been corrected as a result of our quality control procedures. The original label was 'p.[Lys373Gln;Lys382Gln]' xenla-animal_cap Xenopus laevis animal cap animal_cap Animal cap Xenopus laevis animal cap cells are cells situated around the animal (pigmented) pole of a blastula or very early gastrula-stage embryo. This tissue is fated to become cement gland/neurectoderm on the dorsal side of the embryo and epidermis on the ventral side. Animal caps are composed of pluripotent cells that can be induced to form endodermal, mesodermal, or ectodermal cell types. XAO:0000036. 8 unspecified role unspecified role bait bait physical association physical association 5 D The constitutively active TP53 mutant (K373Q/K382Q) efficiently bound the probe, whereas wild-type TP53 did not bind the probe at high levels. Injection of XFDL-MO (Morpholino antisense oligonucleotide to XFDL156) substantially enhanced binding of wild-type TP53 to the probe. This indicates that endogenous XFDL in the animal cap inhibits wild-type TP53 binding to the TP53 binding element. tp53-mix_2 1 6 unspecified role unspecified role prey prey 7 unspecified role unspecified role bait bait association association 5 E in chromatin immunoprecipitation (ChIP) assays of genomic DNA using the endogenous Mix.2 promoter (Figure 5E), the specific binding of p53 to this site was augmented by coinjection of XFDL-MO (compare lanes 3 and 4) and suppressed by XFDL overexpression Binding of p53 to the Mix.2 promoter was enhanced by coinjection of XFDL-MO (Morpholino antisense oligonucleotides to XFDL) and suppressed by XFDL overexpression. Binding to the promoter of the Mix 2 gene was assayed. tp53-xfdl-3 2 10 unspecified role unspecified role prey prey region flag tag flag tag FLAG-tagged FLAG DYKDDDDKV epitope tag DYKDDDDKV epitope tag FLAG FLAG-tagged undetermined undetermined sequence position undetermined undetermined undetermined sequence position undetermined 9 unspecified role unspecified role bait bait n-terminal Venus 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 region required to bind necessary binding region required to bind deletion analysis deletion analysis certain certain sequence position certain range range physical association physical association S4 B, D The p53 deletion analysis (Figure S4A) showed that the aminoterminal transactivation domain (TAD) was dispensable for the binding to XFDL The end of the tp53 range is given as fuzzy coordinates as it is not clear from Fig. S4 A exactly where the end of the construct is. The last two, (the 13th and 14th), Zn-finger motifs were necessary and sufficient for binding to p53. However, the authors did not give the range for this construct.