Activating Compound | Comment | Organism | Structure |
---|---|---|---|
influenza A virus NS1 protein | influenza A virus infection activates the PI3K/Akt pathway by binding influenza A virus NS1 protein to Val573 of the inter-SH2 domain of the p85beta, but not the p85alpha, regulatory subunit of PI3K. NS1-p85-p110 forms a complex in the cells. The interaction is mediated by the interaction interface between the NS1 SH3 binding motif 1, amino acids 164-167, p85beta Val573, and amino acids 137-142 of NS1, molecular modeling and mechanism, overview. Mutant virus PR8-NS1-141/142 is not able to activate Akt phosphorylation | Mus musculus | |
influenza A virus NS1 protein | influenza A virus infection activates the PI3K/Akt pathway by binding influenza A virus NS1 protein to Val573 of the inter-SH2 domain of the p85beta, but not the p85alpha, regulatory subunit of PI3K. NS1-p85-p110 forms a complex in the cells. The interaction is mediated by the interaction interface between the NS1 SH3 binding motif 1, amino acids 164-167, p85beta Val573, and amino acids 137-142 of NS1, molecular modeling and mechanism, overview. Mutant virus PR8-NS1-141/142 is not able to activate Akt phosphorylation | Bos taurus |
Cloned (Comment) | Organism |
---|---|
expression of His-, FLAG-, or GSt-tagged p85beta in HEK-293T or A-549 cells | Mus musculus |
expression of His-, FLAG-, or GSt-tagged p85beta in HEK-293T or A-549 cells | Bos taurus |
Protein Variants | Comment | Organism |
---|---|---|
M582V | site-directed mutagenesis, the full-length p85alpha isoform inter-SH2 domain mutation enables the mutant PI3K to bind influenza A virus NS1 protein leading to activation of the mutant PI3K enzyme activity, molecular modeling, overview | Mus musculus |
M582V | site-directed mutagenesis, the full-length p85alpha isoform inter-SH2 domain mutation enables the mutant PI3K to bind influenza A virus NS1 protein leading to activation of the mutant PI3K enzyme activity, molecular modeling, overview | Bos taurus |
additional information | construction of chimeras of 85alpha and p85beta iSH2 domain by overlapping PCR using mouse p85beta and bovine p85alpha as templates | Mus musculus |
additional information | construction of chimeras of 85alpha and p85beta iSH2 domain by overlapping PCR using mouse p85beta and bovine p85alpha as templates | Bos taurus |
V573M | site-directed mutagenesis, the p85beta isoform inter-SH2 domain mutation abrogates mutant PI3K binding to influenza A virus NS1 protein, molecular modeling, overview | Mus musculus |
V573M | site-directed mutagenesis, the p85beta isoform inter-SH2 domain mutation abrogates mutant PI3K binding to influenza A virus NS1 protein, molecular modeling, overview | Bos taurus |
Metals/Ions | Comment | Organism | Structure |
---|---|---|---|
Mg2+ | - |
Mus musculus | |
Mg2+ | - |
Bos taurus |
Organism | UniProt | Comment | Textmining |
---|---|---|---|
Bos taurus | - |
- |
- |
Mus musculus | - |
- |
- |
Purification (Comment) | Organism |
---|---|
recombinant tagged proteins by the specific affinity chromatographies | Mus musculus |
recombinant tagged proteins by the specific affinity chromatographies | Bos taurus |
Subunits | Comment | Organism |
---|---|---|
heterodimer | catalytic subunit p110 and regulatory subunit p85 | Mus musculus |
heterodimer | catalytic subunit p110 and regulatory subunit p85 | Bos taurus |
Synonyms | Comment | Organism |
---|---|---|
PI3K | - |
Mus musculus |
PI3K | - |
Bos taurus |
Temperature Optimum [°C] | Temperature Optimum Maximum [°C] | Comment | Organism |
---|---|---|---|
20 | - |
assay at | Mus musculus |
20 | - |
assay at | Bos taurus |
pH Optimum Minimum | pH Optimum Maximum | Comment | Organism |
---|---|---|---|
7.4 | - |
assay at | Mus musculus |
7.4 | - |
assay at | Bos taurus |
Cofactor | Comment | Organism | Structure |
---|---|---|---|
ATP | - |
Mus musculus | |
ATP | - |
Bos taurus |