Q07192
Gene name |
map2k2 (mek2) |
Protein name |
Dual specificity mitogen-activated protein kinase kinase 2 |
Names |
MAP kinase kinase 2, MAPKK 2, MAPK-ERK kinase 2 |
Species |
Xenopus laevis (African clawed frog) |
KEGG Pathway |
|
EC number |
2.7.12.2: Dual-specificity kinases (those acting on Ser/Thr and Tyr residues) |
Protein Class |
|
Descriptions
(Annotation based on sequence homology with P45985)
MAP2K4 encodes for Dual specificity mitogen-activated protein kinase kinase 4, belongs to MAP2Ks family, plays an important role in MAP kinase signal transduction pathway. The activation segment appears in a stable a-helical conformation. Phosphorylation of the activation segment destabilizes the autoinhibited state.
Autoinhibitory domains (AIDs)
Accessory elements
293-315 (Activation loop from InterPro)
Target domain |
149-414 (Protein kinase domain) |
Relief mechanism |
|
Assay |
|
References
- Min X et al. (2009) "The structure of the MAP2K MEK6 reveals an autoinhibitory dimer", Structure (London, England : 1993), 17, 96-104
- Shevchenko E et al. (2020) "The autoinhibited state of MKK4: Phosphorylation, putative dimerization and R134W mutant studied by molecular dynamics simulations", Computational and structural biotechnology journal, 18, 2687-2698
Autoinhibited structure
Activated structure
1 structures for Q07192
| Entry ID | Method | Resolution | Chain | Position | Source |
|---|---|---|---|---|---|
| AF-Q07192-F1 | Predicted | AlphaFoldDB |
No variants for Q07192
| Variant ID(s) | Position | Change | Description | Diseaes Association | Provenance |
|---|---|---|---|---|---|
| No variants for Q07192 | |||||
No associated diseases with Q07192
Functions
| Description | ||
|---|---|---|
| EC Number | 2.7.12.2 | Dual-specificity kinases (those acting on Ser/Thr and Tyr residues) |
| Subcellular Localization |
|
|
| PANTHER Family | ||
| PANTHER Subfamily | ||
| PANTHER Protein Class | ||
| PANTHER Pathway Category | No pathway information available | |
No GO annotations of cellular component
| Name | Definition |
|---|---|
| No GO annotations for cellular component |
5 GO annotations of molecular function
| Name | Definition |
|---|---|
| ATP binding | Binding to ATP, adenosine 5'-triphosphate, a universally important coenzyme and enzyme regulator. |
| MAP kinase kinase activity | Catalysis of the concomitant phosphorylation of threonine (T) and tyrosine (Y) residues in a Thr-Glu-Tyr (TEY) thiolester sequence in a MAP kinase (MAPK) substrate. |
| protein serine kinase activity | Catalysis of the reactions: ATP + protein serine = ADP + protein serine phosphate. |
| protein serine/threonine kinase activity | Catalysis of the reactions: ATP + protein serine = ADP + protein serine phosphate, and ATP + protein threonine = ADP + protein threonine phosphate. |
| protein tyrosine kinase activity | Catalysis of the reaction: ATP + a protein tyrosine = ADP + protein tyrosine phosphate. |
No GO annotations of biological process
| Name | Definition |
|---|---|
| No GO annotations for biological process |
No homologous proteins in AiPD
| UniProt AC | Gene Name | Protein Name | Species | Evidence Code |
|---|---|---|---|---|
| No homologous proteins | ||||
| 10 | 20 | 30 | 40 | 50 | 60 |
| AQWGLLHCSL | HLVANILTMA | TSNPSGSSGS | SAGLGFQGQS | QQHSTVNSMQ | GKRKALKLNF |
| 70 | 80 | 90 | 100 | 110 | 120 |
| ANPAFKSTAK | FTLNPTIQST | HVMHKLDAIR | KLETSYQKQD | LRTSGAKALS | TNEQATKNRL |
| 130 | 140 | 150 | 160 | 170 | 180 |
| ERLRTHSIES | SGKLKLSPEQ | HWDFTAEDLK | DLGEIGRGAY | GSVNKMSHTP | SGQIMAVKRI |
| 190 | 200 | 210 | 220 | 230 | 240 |
| RSTVDEKEQK | QLLMDLDVVM | RSSDCPYIVQ | FYGALFREGD | CWICMELMAT | SFDKFYKYVY |
| 250 | 260 | 270 | 280 | 290 | 300 |
| SFLDDVIPEE | ILGKITLATV | KALNHLKENL | KIIHRDIKPS | NILLDTNGNI | KLCDFGISGQ |
| 310 | 320 | 330 | 340 | 350 | 360 |
| LVDSIAKTRD | AGCRPYMAPE | RIDPSASRQG | YDVRSDVWSL | GITLYELATG | RFPYPKWNSV |
| 370 | 380 | 390 | 400 | 410 | 420 |
| FDQLTQVVKG | DPPQLSNSEE | REFSPSFTSF | VNQCLTKDES | KRPKYKELLK | HPFILMYEER |
| 430 | 440 | ||||
| TVDVAGYVGK | ILEQMPVSPS | SPMYVD |