CATH Classification
| Level | CATH Code | Description |
|---|---|---|
|
1 | Mainly Alpha |
|
1.10 | Orthogonal Bundle |
|
1.10.510 | Transferase(Phosphotransferase); domain 1 |
|
1.10.510.10 | Transferase(Phosphotransferase) domain 1 |
Domain Context
CATH Clusters
| Superfamily | Transferase(Phosphotransferase) domain 1 |
| Functional Family | Mitogen-activated protein kinase 14 |
Enzyme Information
| 2.7.11.24 |
Mitogen-activated protein kinase.
based on mapping to UniProt Q16539
ATP + a protein = ADP + a phosphoprotein.
-!- Phosphorylation of specific tyrosine and threonine residues in the activation loop of this enzyme by EC 2.7.12.2 is necessary for enzyme activation. -!- Once activated, the enzyme phosphorylates target substrates on serine or threonine residues followed by a proline. -!- A distinguishing feature of all MAPKs is the conserved sequence Thr- Xaa-Tyr (TXY). -!- Mitogen-activated protein kinase (MAPK) signal transduction pathways are among the most widespread mechanisms of cellular regulation. -!- Mammalian MAPK pathways can be recruited by a wide variety of stimuli including hormones (e.g. insulin and growth hormone), mitogens (e.g. epidermal growth factor and platelet-derived growth factor), vasoactive peptides (e.g. angiotensin-II and endothelin), inflammatory cytokines of the tumor necrosis factor (TNF) family and environmental stresses such as osmotic shock, ionizing radiation and ischemeic injury. -!- Formerly EC 2.7.1.37.
|
UniProtKB Entries (1)
| Q16539 |
MK14_HUMAN
Homo sapiens
Mitogen-activated protein kinase 14
|
PDB Structure
| PDB | 5MTX |
| External Links | |
| Method | X-RAY DIFFRACTION |
| Organism | |
| Primary Citation |
Design, Synthesis, and Biological Evaluation of Novel Type I(1)/2 p38 alpha MAP Kinase Inhibitors with Excellent Selectivity, High Potency, and Prolonged Target Residence Time by Interfering with the R-Spine.
J. Med. Chem.
|