A4K2T0
Gene name |
STK4 |
Protein name |
Serine/threonine-protein kinase 4 |
Names |
|
Species |
Macaca mulatta (Rhesus macaque) |
KEGG Pathway |
mcc:717730 |
EC number |
2.7.11.1: Protein-serine/threonine kinases |
Protein Class |
|
Descriptions
(Annotation based on sequence homology with Q13043)
The Mst1/2 kinases are cytosolic Ste20-related kinases activated by autophosphorylation. Designated class II GC kinases, Mst1 and Mst2, share 76% sequence identity and contain an N-terminal catalytic domain, followed successively by an autoinhibitory segment and a coiled-coil SARAH domain that mediates hetero- and homo-dimerisation. Mst1 and Mst2 also become activated in cells undergoing apoptosis from a variety of stimuli. The activation mechanism is unclear, however, once activated, both kinases undergo cleavage by caspase3 at sites just carboxy terminal to their catalytic domains. The resultant catalytic polypeptides display an altered substrate specificity and lack their autoinhibitory domain. The caspase-cleaved catalytic fragments are highly and constitutively active with unrestricted nuclear access.
Autoinhibitory domains (AIDs)
Target domain |
|
Relief mechanism |
|
Assay |
cis-regPred |
Accessory elements
166-189 (Activation loop from InterPro)
Target domain |
30-281 (Protein kinase domain) |
Relief mechanism |
|
Assay |
|
Autoinhibited structure
Activated structure
1 structures for A4K2T0
| Entry ID | Method | Resolution | Chain | Position | Source |
|---|---|---|---|---|---|
| AF-A4K2T0-F1 | Predicted | AlphaFoldDB |
No variants for A4K2T0
| Variant ID(s) | Position | Change | Description | Diseaes Association | Provenance |
|---|---|---|---|---|---|
| No variants for A4K2T0 | |||||
No associated diseases with A4K2T0
Functions
| Description | ||
|---|---|---|
| EC Number | 2.7.11.1 | Protein-serine/threonine kinases |
| Subcellular Localization |
|
|
| PANTHER Family | ||
| PANTHER Subfamily | ||
| PANTHER Protein Class | ||
| PANTHER Pathway Category | No pathway information available | |
2 GO annotations of cellular component
| Name | Definition |
|---|---|
| cytoplasm | The contents of a cell excluding the plasma membrane and nucleus, but including other subcellular structures. |
| nucleus | A membrane-bounded organelle of eukaryotic cells in which chromosomes are housed and replicated. In most cells, the nucleus contains all of the cell's chromosomes except the organellar chromosomes, and is the site of RNA synthesis and processing. In some species, or in specialized cell types, RNA metabolism or DNA replication may be absent. |
4 GO annotations of molecular function
| Name | Definition |
|---|---|
| ATP binding | Binding to ATP, adenosine 5'-triphosphate, a universally important coenzyme and enzyme regulator. |
| metal ion binding | Binding to a metal ion. |
| 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. |
6 GO annotations of biological process
| Name | Definition |
|---|---|
| apoptotic process | A programmed cell death process which begins when a cell receives an internal (e.g. DNA damage) or external signal (e.g. an extracellular death ligand), and proceeds through a series of biochemical events (signaling pathway phase) which trigger an execution phase. The execution phase is the last step of an apoptotic process, and is typically characterized by rounding-up of the cell, retraction of pseudopodes, reduction of cellular volume (pyknosis), chromatin condensation, nuclear fragmentation (karyorrhexis), plasma membrane blebbing and fragmentation of the cell into apoptotic bodies. When the execution phase is completed, the cell has died. |
| hippo signaling | The series of molecular signals mediated by the serine/threonine kinase Hippo or one of its orthologs. In Drosophila, Hippo in complex with the scaffold protein Salvador (Sav), phosphorylates and activates Warts (Wts), which in turn phosphorylates and inactivates the Yorkie (Yki) transcriptional activator. The core fly components hippo, sav, wts and mats are conserved in mammals as STK4/3 (MST1/2), SAV1/WW45, LATS1/2 and MOB1. |
| intracellular signal transduction | The process in which a signal is passed on to downstream components within the cell, which become activated themselves to further propagate the signal and finally trigger a change in the function or state of the cell. |
| protein phosphorylation | The process of introducing a phosphate group on to a protein. |
| protein tetramerization | The formation of a protein tetramer, a macromolecular structure consisting of four noncovalently associated identical or nonidentical subunits. |
| regulation of MAPK cascade | Any process that modulates the frequency, rate or extent of signal transduction mediated by the MAP kinase (MAPK) cascade. |
10 homologous proteins in AiPD
| UniProt AC | Gene Name | Protein Name | Species | Evidence Code |
|---|---|---|---|---|
| Q5E9L6 | STK4 | Serine/threonine-protein kinase 4 | Bos taurus (Bovine) | SS |
| Q5ZJK4 | STK4 | Serine/threonine-protein kinase 4 | Gallus gallus (Chicken) | SS |
| Q13188 | STK3 | Serine/threonine-protein kinase 3 | Homo sapiens (Human) | SS |
| Q13043 | STK4 | Serine/threonine-protein kinase 4 | Homo sapiens (Human) | EV |
| Q9JI10 | Stk3 | Serine/threonine-protein kinase 3 | Mus musculus (Mouse) | SS |
| Q9JI11 | Stk4 | Serine/threonine-protein kinase 4 | Mus musculus (Mouse) | PR |
| O54748 | Stk3 | Serine/threonine-protein kinase 3 | Rattus norvegicus (Rat) | SS |
| Q9NB31 | cst-1 | Serine/threonine-protein kinase cst-1 | Caenorhabditis elegans | PR |
| Q6P3Q4 | stk4 | Serine/threonine-protein kinase 4 | Xenopus tropicalis (Western clawed frog) (Silurana tropicalis) | SS |
| Q7ZUQ3 | stk3 | Serine/threonine-protein kinase 3 | Danio rerio (Zebrafish) (Brachydanio rerio) | SS |
| 10 | 20 | 30 | 40 | 50 | 60 |
| METVQLRNPP | RRQLKKLDED | SLTKQPEEVF | DVLEKLGEGS | YGSVYKAIHK | ETGQIVAIKQ |
| 70 | 80 | 90 | 100 | 110 | 120 |
| VPVESDLQEI | IKEISIMQQC | DSPHVVKYYG | SYFKNTDLWI | VMEYCGAGSV | SDIIRLRNKT |
| 130 | 140 | 150 | 160 | 170 | 180 |
| LTEDEIATIL | QSTLKGLEYL | HFMRKIHRDI | KAGNILLNTE | GHAKLADFGV | AGQLTDTMAK |
| 190 | 200 | 210 | 220 | 230 | 240 |
| RNTVIGTPFW | MAPEVIQEIG | YNCVADIWSL | GITAIEMAEG | KPPYADIHPM | RAIFMIPTNP |
| 250 | 260 | 270 | 280 | 290 | 300 |
| PPTFRKPELW | SDNFTDFVKQ | CLVKSPEQRA | TATQLLQHPF | VKSAKGVSIL | RDLINEAMDV |
| 310 | 320 | 330 | 340 | 350 | 360 |
| KLKRQESQQR | EVDQDDEENS | EEDEMDSGTM | VRAVGDEMGT | VRVASTMTDG | ASTMIEHDDT |
| 370 | 380 | 390 | 400 | 410 | 420 |
| LPSQLGTMVI | NTEDEEEEGT | MKRRDETMQP | AKPSFLEYFE | QKEKENQINS | FGKSVPGPLK |
| 430 | 440 | 450 | 460 | 470 | 480 |
| NSSDWKIPQD | GDYEFLKSWT | VEDLQKRLLA | LDPMMEQEIE | EIRQKYQSKR | QPILDAIEAK |
| KRRQQNF |