CATH Classification
| Level | CATH Code | Description |
|---|---|---|
|
3 | Alpha Beta |
|
3.30 | 2-Layer Sandwich |
|
3.30.200 | Phosphorylase Kinase; domain 1 |
|
3.30.200.20 | Phosphorylase Kinase; domain 1 |
Domain Context
CATH Clusters
| Superfamily | Phosphorylase Kinase; domain 1 |
| Functional Family | Non-specific serine/threonine protein kinase |
Enzyme Information
| 2.7.11.26 |
[Tau protein] kinase.
based on mapping to UniProt Q9P0L2
ATP + [tau protein] = ADP + [tau protein] phosphate.
-!- Activated by tubulin. -!- Involved in the formation of paired helical filaments, which are the main fibrous component of all fibrillary lesions in brain and are associated with Alzheimer's disease. -!- Formerly EC 2.7.1.135.
|
| 2.7.11.1 |
Non-specific serine/threonine protein kinase.
based on mapping to UniProt Q9P0L2
ATP + a protein = ADP + a phosphoprotein.
-!- This is a heterogeneous group of serine/threonine protein kinases that do not have an activating compound and are either non-specific or their specificity has not been analyzed to date. -!- Formerly EC 2.7.1.37 and EC 2.7.1.70.
|
UniProtKB Entries (1)
| Q9P0L2 |
MARK1_HUMAN
Homo sapiens
Serine/threonine-protein kinase MARK1
|
PDB Structure
| PDB | 2HAK |
| External Links | |
| Method | X-RAY DIFFRACTION |
| Organism | Escherichia |
| Primary Citation |
Structural variations in the catalytic and ubiquitin-associated domains of microtubule-associated protein/microtubule affinity regulating kinase (MARK) 1 and MARK2
J.Biol.Chem.
|