Q8BTW9
Gene name |
Pak4 (Kiaa1142) |
Protein name |
Serine/threonine-protein kinase PAK 4 |
Names |
p21-activated kinase 4, PAK-4 |
Species |
Mus musculus (Mouse) |
KEGG Pathway |
mmu:70584 |
EC number |
2.7.11.1: Protein-serine/threonine kinases |
Protein Class |
|
Descriptions
(Annotation based on sequence homology with O96013)
PAK4 encodes for Serine/threonine-protein kinase PAK 4, and control many cellular functions, including actin cytoskeleton regulation, cell growth, migration and survival, cytokine signaling. Group II PAKs (PAK4, 5, and 6) harbor well-conserved pseudosubstrate sequences. The N-terminal inhibitory segment of PAK4 contains two pseudopeptide sequences (FTGLPR at 32th and RPKPLV at 49th) that binds to the active site of the kinase domain as a pseudosubstrate. PAKs are activated by the binding of GTP-loaded Cdc42 (or Rac) to the CRIB domain, which disrupts the dimer and unfolds autoinhibitory region. After releasing the autoinhibitory region, the kinase domain is then autophosphorylated for full activation.
Autoinhibitory domains (AIDs)
Target domain |
|
Relief mechanism |
|
Assay |
cis-regPred |
Accessory elements
No accessory elements
Autoinhibited structure
Activated structure
1 structures for Q8BTW9
| Entry ID | Method | Resolution | Chain | Position | Source |
|---|---|---|---|---|---|
| AF-Q8BTW9-F1 | Predicted | AlphaFoldDB |
20 variants for Q8BTW9
| Variant ID(s) | Position | Change | Description | Diseaes Association | Provenance |
|---|---|---|---|---|---|
| rs3413096601 | 112 | H>L | No | EVA | |
| rs3410552574 | 123 | A>S | No | EVA | |
| rs36907942 | 134 | S>G | No | EVA | |
| rs3388890515 | 142 | S>G | No | EVA | |
| rs227381279 | 157 | E>D | No | EVA | |
| rs3388894018 | 213 | T>M | No | EVA | |
| rs226485548 | 257 | S>N | No | EVA | |
| rs3388896720 | 292 | R>H | No | EVA | |
| rs3388887574 | 305 | Q>* | No | EVA | |
| rs3388898895 | 327 | I>V | No | EVA | |
| rs3396930562 | 353 | K>* | No | EVA | |
| rs3397311760 | 386 | S>R | No | EVA | |
| rs3388882537 | 402 | G>D | No | EVA | |
| rs3388892987 | 436 | Q>* | No | EVA | |
| rs3388896381 | 487 | E>* | No | EVA | |
| rs3388873802 | 501 | W>R | No | EVA | |
| rs3388882552 | 513 | G>E | No | EVA | |
| rs3388890525 | 556 | V>M | No | EVA | |
| rs3388896399 | 568 | L>M | No | EVA | |
| rs3388885663 | 582 | S>I | No | EVA |
No associated diseases with Q8BTW9
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 | |
1 GO annotations of cellular component
| Name | Definition |
|---|---|
| cytoplasm | The contents of a cell excluding the plasma membrane and nucleus, but including other subcellular structures. |
4 GO annotations of molecular function
| Name | Definition |
|---|---|
| ATP binding | Binding to ATP, adenosine 5'-triphosphate, a universally important coenzyme and enzyme regulator. |
| protein kinase activity | Catalysis of the phosphorylation of an amino acid residue in a protein, usually according to the reaction: a protein + ATP = a phosphoprotein + ADP. |
| 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. |
9 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. |
| cell cycle | The progression of biochemical and morphological phases and events that occur in a cell during successive cell replication or nuclear replication events. Canonically, the cell cycle comprises the replication and segregation of genetic material followed by the division of the cell, but in endocycles or syncytial cells nuclear replication or nuclear division may not be followed by cell division. |
| cellular response to organic cyclic compound | Any process that results in a change in state or activity of a cell (in terms of movement, secretion, enzyme production, gene expression, etc.) as a result of an organic cyclic compound stimulus. |
| dendritic spine development | The process whose specific outcome is the progression of the dendritic spine over time, from its formation to the mature structure. A dendritic spine is a protrusion from a dendrite and a specialized subcellular compartment involved in synaptic transmission. |
| 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. |
| negative regulation of endothelial cell apoptotic process | Any process that stops, prevents or reduces the frequency, rate or extent of endothelial cell apoptotic process. |
| positive regulation of angiogenesis | Any process that activates or increases angiogenesis. |
| protein phosphorylation | The process of introducing a phosphate group on to a protein. |
| regulation of MAPK cascade | Any process that modulates the frequency, rate or extent of signal transduction mediated by the MAP kinase (MAPK) cascade. |
17 homologous proteins in AiPD
| UniProt AC | Gene Name | Protein Name | Species | Evidence Code |
|---|---|---|---|---|
| Q12469 | SKM1 | Serine/threonine-protein kinase SKM1 | Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast) | PR |
| Q9VXE5 | mbt | Serine/threonine-protein kinase PAK mbt | Drosophila melanogaster (Fruit fly) | PR |
| O96013 | PAK4 | Serine/threonine-protein kinase PAK 4 | Homo sapiens (Human) | EV |
| Q9NQU5 | PAK6 | Serine/threonine-protein kinase PAK 6 | Homo sapiens (Human) | EV |
| Q9P286 | PAK5 | Serine/threonine-protein kinase PAK 5 | Homo sapiens (Human) | EV |
| Q9JI11 | Stk4 | Serine/threonine-protein kinase 4 | Mus musculus (Mouse) | PR |
| Q9JI10 | Stk3 | Serine/threonine-protein kinase 3 | Mus musculus (Mouse) | SS |
| Q3ULB5 | Pak6 | Serine/threonine-protein kinase PAK 6 | Mus musculus (Mouse) | PR |
| Q8C015 | Pak5 | Serine/threonine-protein kinase PAK 5 | Mus musculus (Mouse) | SS |
| Q8CIN4 | Pak2 | Serine/threonine-protein kinase PAK 2 | Mus musculus (Mouse) | SS |
| Q61036 | Pak3 | Serine/threonine-protein kinase PAK 3 | Mus musculus (Mouse) | SS |
| Q9JM52 | Mink1 | Misshapen-like kinase 1 | Mus musculus (Mouse) | PR |
| P83510 | Tnik | Traf2 and NCK-interacting protein kinase | Mus musculus (Mouse) | PR |
| P97820 | Map4k4 | Mitogen-activated protein kinase kinase kinase kinase 4 | Mus musculus (Mouse) | PR |
| O88643 | Pak1 | Serine/threonine-protein kinase PAK 1 | Mus musculus (Mouse) | SS |
| D4A280 | Pak5 | Serine/threonine-protein kinase PAK 5 | Rattus norvegicus (Rat) | SS |
| G5EFU0 | pak-2 | Serine/threonine-protein kinase pak-2 | Caenorhabditis elegans | PR |
| 10 | 20 | 30 | 40 | 50 | 60 |
| MFGKKKKRVE | ISAPSNFEHR | VHTGFDQHEQ | KFTGLPRQWQ | SLIEESARRP | KPLIDPACIT |
| 70 | 80 | 90 | 100 | 110 | 120 |
| SIQPGAPKTI | VRGSKGAKDG | ALTLLLDEFE | NMSVTRSNSL | RRESPPPPAR | AHQENGMLEE |
| 130 | 140 | 150 | 160 | 170 | 180 |
| RAAPARMAPD | KAGSRARATG | HSEAGSGSGD | RRRVGPEKRP | KSSRDGPGGP | QEASRDKRPL |
| 190 | 200 | 210 | 220 | 230 | 240 |
| SGPDVSTPQP | GSLTSGTKLA | AGRPFNTYPR | ADTDHPPRGA | QGEPHTMAPN | GPSATGLAAP |
| 250 | 260 | 270 | 280 | 290 | 300 |
| QSSSSSRPPT | RARGAPSPGV | LGPHASEPQL | APPARALAAP | AVPPAPGPPG | PRSPQREPQR |
| 310 | 320 | 330 | 340 | 350 | 360 |
| VSHEQFRAAL | QLVVDPGDPR | SYLDNFIKIG | EGSTGIVCIA | TVRSSGKLVA | VKKMDLRKQQ |
| 370 | 380 | 390 | 400 | 410 | 420 |
| RRELLFNEVV | IMRDYRHENV | VEMYNSYLVG | DELWVVMEFL | EGGALTDIVT | HTRMNEEQIA |
| 430 | 440 | 450 | 460 | 470 | 480 |
| AVCLAVLQAL | AVLHAQGVIH | RDIKSDSILL | THDGRVKLSD | FGFCAQVSKE | VPRRKSLVGT |
| 490 | 500 | 510 | 520 | 530 | 540 |
| PYWMAPELIS | RLPYGPEVDI | WSLGVMVIEM | VDGEPPYFNE | PPLKAMKMIR | DNLPPRLKNL |
| 550 | 560 | 570 | 580 | 590 | |
| HKASPSLKGF | LDRLLVRDPA | QRATAAELLK | HPFLTKAGPP | ASIVPLMRQH | RTR |