Any feedback?
Literature summary for 2.7.1.153 extracted from
- Mechanism of influenza A virus NS1 protein interaction with the p85beta, but not the p85alpha, subunit of phosphatidylinositol 3-kinase (PI3K) and up-regulation of PI3K activity (2008), J. Biol. Chem., 283, 23397-23409.
Activating Compound
| 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(Commentary)
| 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
| 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
| Metals/Ions | Comment | Organism | Structure |
|---|---|---|---|
| Mg2+ | - |
Mus musculus |  |
| Mg2+ | - |
Bos taurus | |
Organism
| Organism | UniProt | Comment | Textmining |
|---|---|---|---|
| Bos taurus | - |
- |
- |
| Mus musculus | - |
- |
- |
Purification (Commentary)
| Purification (Comment) | Organism |
|---|---|
| recombinant tagged proteins by the specific affinity chromatographies | Mus musculus |
| recombinant tagged proteins by the specific affinity chromatographies | Bos taurus |
Subunits
| Subunits | Comment | Organism |
|---|---|---|
| heterodimer | catalytic subunit p110 and regulatory subunit p85 | Mus musculus |
| heterodimer | catalytic subunit p110 and regulatory subunit p85 | Bos taurus |
Synonyms
| Synonyms | Comment | Organism |
|---|---|---|
| PI3K | - |
Mus musculus |
| PI3K | - |
Bos taurus |
Temperature Optimum [°C]
| Temperature Optimum [°C] | Temperature Optimum Maximum [°C] | Comment | Organism |
|---|---|---|---|
| 20 | - |
assay at | Mus musculus |
| 20 | - |
assay at | Bos taurus |
pH Optimum
| pH Optimum Minimum | pH Optimum Maximum | Comment | Organism |
|---|---|---|---|
| 7.4 | - |
assay at | Mus musculus |
| 7.4 | - |
assay at | Bos taurus |
Cofactor
| Cofactor | Comment | Organism | Structure |
|---|---|---|---|
| ATP | - |
Mus musculus | |
| ATP | - |
Bos taurus | |
Use of this online version of BRENDA is free under the CC BY 4.0 license. See terms of use for full details.
Release 2023.1 (January 2023)
Legal
Curated at
Member of
