I2D I2D Dual-specificity phosphatase 26 is a novel p53 phosphatase and inhibits p53 tumor suppressor functions in human neuroblastoma. Dual-specificity phosphatase 26 is a novel p53 phosphatase and inhibits p53 tumor suppressor functions in human neuroblastoma. Oncogene (0950-9232) 2010 imex curation Shang X., Vasudevan SA., Yu Y., Ge N., Ludwig AD., Wesson CL., Wang K., Burlingame SM., Zhao YJ., Rao PH., Lu X., Russell HV., Okcu MF., Hicks MJ., Shohet JM., Donehower LA., Nuchtern JG., Yang J. Apoptosis - Interactions involving proteins with a function related to apoptosis Cancer - Interactions investigated in the context of cancer Confirmed by author: all p53 constructs are of human origin. jianhuay@bcm.edu 21-Dec-2010: Contacted by JYOTI. orchard Only protein-protein interactions Curated by: I2D - Interologous Interaction Database in vitro In vitro pull down pull down western blot western blot Immuno blot Immuno blot Shang X., Vasudevan SA., Yu Y., Ge N., Ludwig AD., Wesson CL., Wang K., Burlingame SM., Zhao YJ., Rao PH., Lu X., Russell HV., Okcu MF., Hicks MJ., Shohet JM., Donehower LA., Nuchtern JG., Yang J. Apoptosis - Interactions involving proteins with a function related to apoptosis Confirmed by author: all p53 constructs are of human origin. jianhuay@bcm.edu Accepted 2010-NOV-4 by ORCHARD. 21-Dec-2010: Contacted by JYOTI. Oncogene (0950-9232) 2010 orchard Only protein-protein interactions imex curation Curated by: I2D - Interologous Interaction Database Dual-specificity phosphatase 26 is a novel p53 phosphatase and inhibits p53 tumor suppressor functions in human neuroblastoma. Dual-specificity phosphatase 26 is a novel p53 phosphatase and inhibits p53 tumor suppressor functions in human neuroblastoma. Oncogene (0950-9232) 2010 imex curation Shang X., Vasudevan SA., Yu Y., Ge N., Ludwig AD., Wesson CL., Wang K., Burlingame SM., Zhao YJ., Rao PH., Lu X., Russell HV., Okcu MF., Hicks MJ., Shohet JM., Donehower LA., Nuchtern JG., Yang J. Apoptosis - Interactions involving proteins with a function related to apoptosis Cancer - Interactions investigated in the context of cancer Confirmed by author: all p53 constructs are of human origin. jianhuay@bcm.edu 21-Dec-2010: Contacted by JYOTI. orchard Only protein-protein interactions Curated by: I2D - Interologous Interaction Database human-sh_sy5y Homo sapiens SH-SY5Y cell line sh_sy5y Human neuroblastoma cells anti bait coip anti bait coimmunoprecipitation anti bait coip western blot western blot Immuno blot Immuno blot Shang X., Vasudevan SA., Yu Y., Ge N., Ludwig AD., Wesson CL., Wang K., Burlingame SM., Zhao YJ., Rao PH., Lu X., Russell HV., Okcu MF., Hicks MJ., Shohet JM., Donehower LA., Nuchtern JG., Yang J. Apoptosis - Interactions involving proteins with a function related to apoptosis Confirmed by author: all p53 constructs are of human origin. jianhuay@bcm.edu Accepted 2010-NOV-4 by ORCHARD. 21-Dec-2010: Contacted by JYOTI. Oncogene (0950-9232) 2010 orchard Only protein-protein interactions imex curation Curated by: I2D - Interologous Interaction Database Dual-specificity phosphatase 26 is a novel p53 phosphatase and inhibits p53 tumor suppressor functions in human neuroblastoma. Dual-specificity phosphatase 26 is a novel p53 phosphatase and inhibits p53 tumor suppressor functions in human neuroblastoma. Oncogene (0950-9232) 2010 imex curation Shang X., Vasudevan SA., Yu Y., Ge N., Ludwig AD., Wesson CL., Wang K., Burlingame SM., Zhao YJ., Rao PH., Lu X., Russell HV., Okcu MF., Hicks MJ., Shohet JM., Donehower LA., Nuchtern JG., Yang J. Apoptosis - Interactions involving proteins with a function related to apoptosis Cancer - Interactions investigated in the context of cancer Confirmed by author: all p53 constructs are of human origin. jianhuay@bcm.edu 21-Dec-2010: Contacted by JYOTI. orchard Only protein-protein interactions Curated by: I2D - Interologous Interaction Database in vitro In vitro phosphatase assay phosphatase assay tag fluorescence tag visualisation by fluorescence tag fluorescence Shang X., Vasudevan SA., Yu Y., Ge N., Ludwig AD., Wesson CL., Wang K., Burlingame SM., Zhao YJ., Rao PH., Lu X., Russell HV., Okcu MF., Hicks MJ., Shohet JM., Donehower LA., Nuchtern JG., Yang J. Apoptosis - Interactions involving proteins with a function related to apoptosis Phosphatase activity was measured in pmols/min by absorbance at 600nm of free phosphate in a malachite green/molybdate-based assay Confirmed by author: all p53 constructs are of human origin. jianhuay@bcm.edu Accepted 2010-NOV-4 by ORCHARD. 21-Dec-2010: Contacted by JYOTI. Oncogene (0950-9232) 2010 orchard Only protein-protein interactions imex curation Curated by: I2D - Interologous Interaction Database Dual-specificity phosphatase 26 is a novel p53 phosphatase and inhibits p53 tumor suppressor functions in human neuroblastoma. Dual-specificity phosphatase 26 is a novel p53 phosphatase and inhibits p53 tumor suppressor functions in human neuroblastoma. Oncogene (0950-9232) 2010 imex curation Shang X., Vasudevan SA., Yu Y., Ge N., Ludwig AD., Wesson CL., Wang K., Burlingame SM., Zhao YJ., Rao PH., Lu X., Russell HV., Okcu MF., Hicks MJ., Shohet JM., Donehower LA., Nuchtern JG., Yang J. Apoptosis - Interactions involving proteins with a function related to apoptosis Cancer - Interactions investigated in the context of cancer Confirmed by author: all p53 constructs are of human origin. jianhuay@bcm.edu 21-Dec-2010: Contacted by JYOTI. orchard Only protein-protein interactions Curated by: I2D - Interologous Interaction Database 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 Shang X., Vasudevan SA., Yu Y., Ge N., Ludwig AD., Wesson CL., Wang K., Burlingame SM., Zhao YJ., Rao PH., Lu X., Russell HV., Okcu MF., Hicks MJ., Shohet JM., Donehower LA., Nuchtern JG., Yang J. Apoptosis - Interactions involving proteins with a function related to apoptosis Confirmed by author: all p53 constructs are of human origin. jianhuay@bcm.edu Accepted 2010-NOV-4 by ORCHARD. 21-Dec-2010: Contacted by JYOTI. Oncogene (0950-9232) 2010 orchard Only protein-protein interactions imex curation Curated by: I2D - Interologous Interaction Database Dual-specificity phosphatase 26 is a novel p53 phosphatase and inhibits p53 tumor suppressor functions in human neuroblastoma. Dual-specificity phosphatase 26 is a novel p53 phosphatase and inhibits p53 tumor suppressor functions in human neuroblastoma. Oncogene (0950-9232) 2010 imex curation Shang X., Vasudevan SA., Yu Y., Ge N., Ludwig AD., Wesson CL., Wang K., Burlingame SM., Zhao YJ., Rao PH., Lu X., Russell HV., Okcu MF., Hicks MJ., Shohet JM., Donehower LA., Nuchtern JG., Yang J. Apoptosis - Interactions involving proteins with a function related to apoptosis Cancer - Interactions investigated in the context of cancer Confirmed by author: all p53 constructs are of human origin. jianhuay@bcm.edu 21-Dec-2010: Contacted by JYOTI. orchard Only protein-protein interactions Curated by: I2D - Interologous Interaction Database human-imr_32 Homo sapiens:Neuroblastoma cell line imr_32 Human IMR-32 Neuroblastoma Human neuroblastoma cell line established from an abdominal mass (diagnosed as neuroblastoma) of a 1-year-old Caucasian boy in 1967. anti bait coip anti bait coimmunoprecipitation anti bait coip western blot western blot Immuno blot Immuno blot Shang X., Vasudevan SA., Yu Y., Ge N., Ludwig AD., Wesson CL., Wang K., Burlingame SM., Zhao YJ., Rao PH., Lu X., Russell HV., Okcu MF., Hicks MJ., Shohet JM., Donehower LA., Nuchtern JG., Yang J. Apoptosis - Interactions involving proteins with a function related to apoptosis Confirmed by author: all p53 constructs are of human origin. jianhuay@bcm.edu Accepted 2010-NOV-4 by ORCHARD. 21-Dec-2010: Contacted by JYOTI. Oncogene (0950-9232) 2010 orchard Only protein-protein interactions imex curation Curated by: I2D - Interologous Interaction Database Dual-specificity phosphatase 26 is a novel p53 phosphatase and inhibits p53 tumor suppressor functions in human neuroblastoma. Dual-specificity phosphatase 26 is a novel p53 phosphatase and inhibits p53 tumor suppressor functions in human neuroblastoma. Oncogene (0950-9232) 2010 imex curation Shang X., Vasudevan SA., Yu Y., Ge N., Ludwig AD., Wesson CL., Wang K., Burlingame SM., Zhao YJ., Rao PH., Lu X., Russell HV., Okcu MF., Hicks MJ., Shohet JM., Donehower LA., Nuchtern JG., Yang J. Apoptosis - Interactions involving proteins with a function related to apoptosis Cancer - Interactions investigated in the context of cancer Confirmed by author: all p53 constructs are of human origin. jianhuay@bcm.edu 21-Dec-2010: Contacted by JYOTI. orchard Only protein-protein interactions Curated by: I2D - Interologous Interaction Database 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 bait coip anti bait coimmunoprecipitation anti bait coip anti tag western anti tag western blot anti tag western Shang X., Vasudevan SA., Yu Y., Ge N., Ludwig AD., Wesson CL., Wang K., Burlingame SM., Zhao YJ., Rao PH., Lu X., Russell HV., Okcu MF., Hicks MJ., Shohet JM., Donehower LA., Nuchtern JG., Yang J. Apoptosis - Interactions involving proteins with a function related to apoptosis Confirmed by author: all p53 constructs are of human origin. jianhuay@bcm.edu Accepted 2010-NOV-4 by ORCHARD. 21-Dec-2010: Contacted by JYOTI. Oncogene (0950-9232) 2010 orchard Only protein-protein interactions imex curation Curated by: I2D - Interologous Interaction Database dus26_human Dual specificity protein phosphatase 26 DUSP26 DUSP24 LDP4 MKP8 NATA1 SKRP3 Low-molecular-mass dual-specificity phosphatase 4 Mitogen-activated protein kinase phosphatase 8 Novel amplified gene in thyroid anaplastic cancer Dual specificity phosphatase SKRP3 protein protein human Homo sapiens Human MCPGNWLWASMTFMARFSRSSSRSPVRTRGTLEEMPTVQHPFLNVFELERLLYTGKTACNHADEVWPGLYLGDQDMANNRRELRRLGITHVLNASHSRWRGTPEAYEGLGIRYLGVEAHDSPAFDMSIHFQTAADFIHRALSQPGGKILVHCAVGVSRSATLVLAYLMLYHHLTLVEAIKKVKDHRGIIPNRGFLRQLLALDRRLRQGLEA 60E944304905086D 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 dusp26-p53-1 4 8 unspecified role unspecified role prey prey 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 7 unspecified role unspecified role bait bait 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 physical association physical association Fig. 4c dusp26-p53-2 1 8 unspecified role unspecified role prey prey 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 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. 7 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 Q9BV47:p.Cys152Ser mutation mutation certain certain sequence position certain certain certain sequence position certain C S Wed May 02 20:04:57 BST 2018 This feature has been corrected as a result of our quality control procedures. The original label was 'cys152ser' Tue Jun 30 16:15:49 BST 2020 This feature has been corrected as a result of our quality control procedures. The original label was 'p.Cys152Ser' ecoli Escherichia coli (strain K12) direct interaction direct interaction Fig. 4d, S4b DUSP26-CS mutant still binds p53 suggesting that phosphatase activity of DUSP26 not required to bind p53. dusp26-p53-3 1 8 unspecified role unspecified role prey prey 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) 7 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 ecoli Escherichia coli (strain K12) direct interaction direct interaction Fig. 4e dusp26-p53-4 5 8 unspecified role unspecified role bait bait 7 unspecified role unspecified role prey prey physical association physical association Fig. 4f dusp26-p53-5 3 8 enzyme target enzyme target substrate substrate bait bait region identified peptide identified peptide certain certain sequence position certain certain certain sequence position certain ser15 opser O-phospho-L-serine (2S)-2-amino-3-(phosphonooxy)propanoic acid 2-amino-3-hydroxypropanoic acid 3-phosphate 2-azanyl-3-(phosphonooxy)propanoic acid ACT_SITE Phosphoserine intermediate MOD_RES Phosphoserine O-phospho-L-serine O-phosphonoserine O-phosphorylated L-serine O3-phosphoserine serine phosphate ester OPSer Phospho Phospho Seryl Phosphorylation phosphorylations predetermined featur predetermined feature predetermined featur certain certain sequence position certain certain certain sequence position certain 7 enzyme enzyme prey prey Q9BV47:p.Cys152Ser Alters kinetics of interaction mutation mutation certain certain sequence position certain certain certain sequence position certain C S Wed May 02 18:11:09 BST 2018 This feature has been corrected as a result of our quality control procedures. The original label was 'cys152ser' Tue Jun 30 19:24:52 BST 2020 This feature has been corrected as a result of our quality control procedures. The original label was 'p.Cys152Ser' ecoli Escherichia coli (strain K12) dephosphorylation dephosphorylation reaction dephosphorylation Fig. 4g dusp26-p53-8 6 8 unspecified role unspecified role bait bait 7 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 physical association physical association Fig. S4a dusp26-p53-9 2 8 unspecified role unspecified role prey prey 7 unspecified role unspecified role bait bait physical association physical association Supp. Fig. 5b dusp26-p53-7 3 8 enzyme target enzyme target substrate substrate bait bait region identified peptide identified peptide certain certain sequence position certain certain certain sequence position certain ser37 Undetermined feature position opser O-phospho-L-serine (2S)-2-amino-3-(phosphonooxy)propanoic acid 2-amino-3-hydroxypropanoic acid 3-phosphate 2-azanyl-3-(phosphonooxy)propanoic acid ACT_SITE Phosphoserine intermediate MOD_RES Phosphoserine O-phospho-L-serine O-phosphonoserine O-phosphorylated L-serine O3-phosphoserine serine phosphate ester OPSer Phospho Phospho Seryl Phosphorylation phosphorylations predetermined featur predetermined feature predetermined featur certain certain sequence position certain certain certain sequence position certain 7 enzyme enzyme prey prey Q9BV47:p.Cys152Ser Alters kinetics of interaction mutation mutation certain certain sequence position certain certain certain sequence position certain C S Wed May 02 16:36:22 BST 2018 This feature has been corrected as a result of our quality control procedures. The original label was 'cys152ser' Tue Jun 30 18:19:11 BST 2020 This feature has been corrected as a result of our quality control procedures. The original label was 'p.Cys152Ser' ecoli Escherichia coli (strain K12) dephosphorylation dephosphorylation reaction dephosphorylation Fig. 4g dusp26-p53-6 3 8 enzyme target enzyme target substrate substrate bait bait region identified peptide identified peptide certain certain sequence position certain certain certain sequence position certain ser20 opser O-phospho-L-serine (2S)-2-amino-3-(phosphonooxy)propanoic acid 2-amino-3-hydroxypropanoic acid 3-phosphate 2-azanyl-3-(phosphonooxy)propanoic acid ACT_SITE Phosphoserine intermediate MOD_RES Phosphoserine O-phospho-L-serine O-phosphonoserine O-phosphorylated L-serine O3-phosphoserine serine phosphate ester OPSer Phospho Phospho Seryl Phosphorylation phosphorylations predetermined featur predetermined feature predetermined featur certain certain sequence position certain certain certain sequence position certain 7 enzyme enzyme prey prey Q9BV47:p.Cys152Ser Alters kinetics of interaction mutation mutation certain certain sequence position certain certain certain sequence position certain C S Wed May 02 20:31:03 BST 2018 This feature has been corrected as a result of our quality control procedures. The original label was 'cys152ser' Tue Jun 30 19:53:23 BST 2020 This feature has been corrected as a result of our quality control procedures. The original label was 'p.Cys152Ser' ecoli Escherichia coli (strain K12) dephosphorylation dephosphorylation reaction dephosphorylation Fig. 4g