| Unique identifier for interactor A | uniprotkb:P29074 |
| Unique identifier for interactor B | uniprotkb:P53778 |
| Alternative identifier for interactor A | intact:EBI-710431 uniprotkb:B2RBV8 uniprotkb:Q9UDA7 ensembl:ENSP00000263708.2 |
| Alternative identifier for interactor B | intact:EBI-602406 uniprotkb:Q6IC53 uniprotkb:Q14260 uniprotkb:Q99588 uniprotkb:Q99672 ensembl:ENSP00000215659.8 |
| Aliases for A | psi-mi:ptn4_human(display_long) uniprotkb:Protein-tyrosine phosphatase MEG1(gene name synonym) uniprotkb:PTPN4(gene name) psi-mi:PTPN4(display_short) |
| Aliases for B | psi-mi:mk12_human(display_long) uniprotkb:Extracellular signal-regulated kinase 6(gene name synonym) uniprotkb:Stress-activated protein kinase 3(gene name synonym) uniprotkb:Mitogen-activated protein kinase p38 gamma(gene name synonym) uniprotkb:MAPK12(gene name) psi-mi:MAPK12(display_short) uniprotkb:ERK6(gene name synonym) uniprotkb:SAPK3(gene name synonym) |
| Interaction detection methods | psi-mi:"MI:0415"(enzymatic study) |
| First author | Maisonneuve et al. (2014) |
| Identifier of the publication | imex:IM-23056 pubmed:25158884 |
| NCBI Taxonomy identifier for interactor A | taxid:9606(human) taxid:9606(Homo sapiens) |
| NCBI Taxonomy identifier for interactor B | taxid:9606(human) taxid:9606(Homo sapiens) |
| Interaction types | psi-mi:"MI:0203"(dephosphorylation reaction) |
| Source databases and identifiers | psi-mi:"MI:0471"(MINT) |
| Interaction identifier(s) in the corresponding source database | intact:EBI-9681802 imex:IM-23056-2 |
| Confidence score | intact-miscore:0.44 |
| Complex expansion | - |
| Biological role A | Enzyme |
| Biological role B | Enzyme target |
| Experimental role A | Neutral component |
| Experimental role B | Neutral component |
| Interactor type A | Protein |
| Interactor type B | Protein |
| Annotations for the interaction | figure legend:f1b t1 comment:"\"Both linker-PTP and PDZ-PTPWT dephosphorylated the pTyr substrate following Michaelis-Menten kinetics (Fig. 1B). The Michaelis constant (KM) and the turnover number (kcat) values were deduced by fitting the experimental data to the Michaelis-Menten equation (Table 1). The kcat and KM values decreased by 6.5 fold and by 3.8 fold, respectively, when comparing linker-PTP and PDZ-PTPWT. The compensatory effects between kcat and KM explain the small change in the kcat/KM ratio of 1.7 fold (Table 1).\"" curation depth:imex curation full coverage:Only protein-protein interactions |
| NCBI Taxonomy identifier for the host organism | taxid:-1(in vitro) taxid:-1(In vitro) |
| Parameters of the interaction | kd:4.3x10^-6(molar) |
| Creation date | 2014/07/28 |
| Update date | 2024/11/30 |
| negative Boolean value | false |
| Feature(s) for interactor A | glutathione s tranferase tag:?-? binding-associated region:499-926 |
| Feature(s) for interactor B | binding-associated region:178-189 |
| Stoichiometry for interactor A | - |
| Stoichiometry for interactor B | - |
| Participant identification method for interactor A | Predetermined participant |
| Participant identification method for interactor B | Peptide synthesis |