Cloned (Comment) | Organism |
---|---|
recombinant expression of C-terminally His6-tagged p38alpha in Escherichia coli strain BL21 (DE3) RIL | Homo sapiens |
Organism | UniProt | Comment | Textmining |
---|---|---|---|
Homo sapiens | Q16539 | - |
- |
Purification (Comment) | Organism |
---|---|
recombinant C-terminally His6-tagged p38alpha from Escherichia coli strain BL21 (DE3) RIL by nickel affinity chromatography and gel filtration | Homo sapiens |
Synonyms | Comment | Organism |
---|---|---|
MAPK14 | - |
Homo sapiens |
p38alpha | - |
Homo sapiens |
General Information | Comment | Organism |
---|---|---|
additional information | regulation of MAPKs is achieved via a plethora of regulatory proteins including activating MAPKKs and an abundance of deactivating phosphatases. Although all regulatory proteins use an identical interaction site on MAPKs, the common docking and hydrophobic pocket, they use distinct kinase interaction motif (KIM or D-motif) sequences that are present in linear, peptide-like, or well folded protein domains. Fine-tuning necessary to achieve MAPK specificity and regulation among multiple regulatory proteins | Homo sapiens |
physiological function | dual specificity phosphatases play a crucial role in MAP kinase regulation. Dual specificity phosphatase DUSP16 (MKP7) and p38alpha interact in a unique manner that is different from other dual specificity phosphatases, DUSP16 binds p38alpha via an extended binding surface that includes helix alpha4. KIM-containing MAPK-specific dual specificity phosphatase DUSP10 also uses a unique binding mode to interact with p38alpha. The interaction of the MAPK binding domain of DUSP16 with p38alpha shows that despite belonging to the same dual specificity phosphatase (DUSP) family, its interaction mode differs from that of DUSP10, detailed overview. DUSP16 selectively inactivates JNK and p38 following stress activation | Homo sapiens |