G5EFU0
Gene name |
pak-2 |
Protein name |
Serine/threonine-protein kinase pak-2 |
Names |
p21-activated kinase 2 |
Species |
Caenorhabditis elegans |
KEGG Pathway |
cel:CELE_C45B11.1 |
EC number |
2.7.11.1: Protein-serine/threonine kinases |
Protein Class |
|
Descriptions
(Annotation based on sequence homology with Q9NQU5)
The p21-activated protein kinases5 (PAK5) belongs to group II PAK family and is involved in actin cytoskeleton regulation, cell growth, migration and survival, and so on. Group II PAKs (PAK4, 5, and 6) harbor well-conserved pseudosubstrate sequences. For PAK4, the N-terminal inhibitory segment contains two pseudopeptide sequences (FTGLPR at 32th and RPKPLV at 49th) that bind to the active site of the kinase domain as a pseudosubstrate. Like PAK4, PAK6 catalytic activity is inhibited by a peptide corresponding to its N-terminal pseudosubstrate (RRPKPVVDP at 49th).
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 autoinhibitory region, 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 G5EFU0
| Entry ID | Method | Resolution | Chain | Position | Source |
|---|---|---|---|---|---|
| AF-G5EFU0-F1 | Predicted | AlphaFoldDB |
No variants for G5EFU0
| Variant ID(s) | Position | Change | Description | Diseaes Association | Provenance |
|---|---|---|---|---|---|
| No variants for G5EFU0 | |||||
No associated diseases with G5EFU0
5 regional properties for G5EFU0
| Type | Name | Position | InterPro Accession |
|---|---|---|---|
| domain | Protein kinase domain | 681 - 956 | IPR000719 |
| domain | Serine-threonine/tyrosine-protein kinase, catalytic domain | 684 - 952 | IPR001245 |
| active_site | Serine/threonine-protein kinase, active site | 803 - 815 | IPR008271 |
| binding_site | Protein kinase, ATP binding site | 687 - 709 | IPR017441 |
| domain | Malectin domain | 417 - 604 | IPR021720 |
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. |
| 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. |
4 GO annotations of biological process
| Name | Definition |
|---|---|
| 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. |
| nematode larval development | The process whose specific outcome is the progression of the nematode larva over time, from its formation to the mature structure. Nematode larval development begins with the newly hatched first-stage larva (L1) and ends with the end of the last larval stage (for example the fourth larval stage (L4) in C. elegans). Each stage of nematode larval development is characterized by proliferation of specific cell lineages and an increase in body size without alteration of the basic body plan. Nematode larval stages are separated by molts in which each stage-specific exoskeleton, or cuticle, is shed and replaced anew. |
| 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. |
23 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 |
| Q08E52 | PAK1 | Serine/threonine-protein kinase PAK 1 | Bos taurus (Bovine) | SS |
| Q7YQL4 | PAK3 | Serine/threonine-protein kinase PAK 3 | Pan troglodytes (Chimpanzee) | SS |
| Q9VXE5 | mbt | Serine/threonine-protein kinase PAK mbt | Drosophila melanogaster (Fruit fly) | PR |
| Q13153 | PAK1 | Serine/threonine-protein kinase PAK 1 | Homo sapiens (Human) | EV |
| Q13177 | PAK2 | Serine/threonine-protein kinase PAK 2 | Homo sapiens (Human) | EV |
| O75914 | PAK3 | Serine/threonine-protein kinase PAK 3 | Homo sapiens (Human) | SS |
| Q9NQU5 | PAK6 | Serine/threonine-protein kinase PAK 6 | Homo sapiens (Human) | EV |
| O96013 | PAK4 | Serine/threonine-protein kinase PAK 4 | Homo sapiens (Human) | EV |
| Q9P286 | PAK5 | Serine/threonine-protein kinase PAK 5 | Homo sapiens (Human) | EV |
| Q8CIN4 | Pak2 | Serine/threonine-protein kinase PAK 2 | Mus musculus (Mouse) | SS |
| O88643 | Pak1 | Serine/threonine-protein kinase PAK 1 | Mus musculus (Mouse) | SS |
| Q61036 | Pak3 | Serine/threonine-protein kinase PAK 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 |
| Q8BTW9 | Pak4 | Serine/threonine-protein kinase PAK 4 | Mus musculus (Mouse) | PR |
| Q62829 | Pak3 | Serine/threonine-protein kinase PAK 3 | Rattus norvegicus (Rat) | SS |
| Q64303 | Pak2 | Serine/threonine-protein kinase PAK 2 | Rattus norvegicus (Rat) | SS |
| P35465 | Pak1 | Serine/threonine-protein kinase PAK 1 | Rattus norvegicus (Rat) | SS |
| D4A280 | Pak5 | Serine/threonine-protein kinase PAK 5 | Rattus norvegicus (Rat) | SS |
| G5EGQ3 | max-2 | Serine/threonine-protein kinase max-2 | Caenorhabditis elegans | SS |
| Q17850 | pak-1 | Serine/threonine-protein kinase pak-1 | Caenorhabditis elegans | PR |
| Q9NB31 | cst-1 | Serine/threonine-protein kinase cst-1 | Caenorhabditis elegans | PR |
| 10 | 20 | 30 | 40 | 50 | 60 |
| MNRTFSLRRK | VKKSEISTPS | NFEHRIHAGF | DARSGTYTGL | PKQWQALLGP | PRSISRPKPM |
| 70 | 80 | 90 | 100 | 110 | 120 |
| VDPSCITPVD | VAELKTVIRG | PSSSFRYNSP | LPFGMTNSPM | PSVARSNSLR | ISATASPVVN |
| 130 | 140 | 150 | 160 | 170 | 180 |
| VSSARHSFRP | TLPPVSQRGY | PFNDPSYAPL | PLRNQKPPMS | TTFGVEKPHQ | YQQIITIVAP |
| 190 | 200 | 210 | 220 | 230 | 240 |
| SRTTTPQLQP | KSPSTPQAMR | QQPKCTEGVS | DEEFRNALKF | VVDGTDPRSD | LTDYKQIGEG |
| 250 | 260 | 270 | 280 | 290 | 300 |
| STGVVEAAYK | ISTKQIVAVK | RMNLRKQQRR | ELLFNEVSIL | RQYQHPNIVR | FFSSHLVDDE |
| 310 | 320 | 330 | 340 | 350 | 360 |
| LWVVMEFMEG | GSLTDIVTAT | RMTEPQIATI | SRQVLGALDF | LHARKVIHRD | IKSDSILLKR |
| 370 | 380 | 390 | 400 | 410 | 420 |
| DGTVKLTDFG | FCGQLSEEVP | RRRSLVGTPY | WTAAEVIARE | PYDTRADIWS | FGIMLIEMVE |
| 430 | 440 | 450 | 460 | 470 | 480 |
| GEPPFFNDQP | FQAMKRIRDE | HEARFSRHAK | VSVELSELLS | HCIVKDVNKR | WPAKDLLRHP |
| 490 | 500 | 510 | 520 | ||
| FFAKAQHSSS | IAPLLLQLQG | NTINGNNPPT | HHHSSQITTV | IQ |