Q9NES8
Gene name |
pph-5 |
Protein name |
Serine/threonine-protein phosphatase 5 |
Names |
|
Species |
Caenorhabditis elegans |
KEGG Pathway |
|
EC number |
3.1.3.16: Phosphoric monoester hydrolases |
Protein Class |
SERINE/THREONINE-PROTEIN PHOSPHATASE 5-RELATED (PTHR45668) |
Descriptions
Protein phosphatase 5 is involved in the regulation of kinases and transcription factors. Its dephosphorylation activity is modulated by the C-terminal MEEVD motif of molecular chaperone Hsp90, which binds to the tetratricopeptide repeat (TPR) domain of protein phosphatase 5. The TRP domain is involved in autoinhibition and the addition of a peptide containing the MEEVD motif counteracts the autoinhibition of the TPR domain.
Autoinhibitory domains (AIDs)
Target domain |
156-495 (Phosphatase domain) |
Relief mechanism |
Partner binding |
Assay |
Structural analysis |
Accessory elements
No accessory elements
References
- Haslbeck V et al. (2015) "The activity of protein phosphatase 5 towards native clients is modulated by the middle- and C-terminal domains of Hsp90", Scientific reports, 5, 17058
- Chen MX et al. (1997) "Activation of protein phosphatase 5 by limited proteolysis or the binding of polyunsaturated fatty acids to the TPR domain", FEBS letters, 400, 136-40
Autoinhibited structure
Activated structure
1 structures for Q9NES8
| Entry ID | Method | Resolution | Chain | Position | Source |
|---|---|---|---|---|---|
| AF-Q9NES8-F1 | Predicted | AlphaFoldDB |
No variants for Q9NES8
| Variant ID(s) | Position | Change | Description | Diseaes Association | Provenance |
|---|---|---|---|---|---|
| No variants for Q9NES8 | |||||
No associated diseases with Q9NES8
6 regional properties for Q9NES8
| Type | Name | Position | InterPro Accession |
|---|---|---|---|
| domain | Protein kinase domain | 16 - 268 | IPR000719 |
| active_site | Serine/threonine-protein kinase, active site | 135 - 147 | IPR008271 |
| binding_site | Protein kinase, ATP binding site | 22 - 45 | IPR017441 |
| domain | PRKAA2, UBA-like autoinhibitory domain | 285 - 349 | IPR028783 |
| domain | AMPK, C-terminal adenylate sensor domain | 401 - 479 | IPR032270 |
| domain | 5'-AMP-activated protein kinase catalytic subunit alpha-2, C-terminal | 395 - 550 | IPR039148 |
Functions
| Description | ||
|---|---|---|
| EC Number | 3.1.3.16 | Phosphoric monoester hydrolases |
| Subcellular Localization |
|
|
| PANTHER Family | PTHR45668 | SERINE/THREONINE-PROTEIN PHOSPHATASE 5-RELATED |
| PANTHER Subfamily | PTHR45668:SF5 | SERINE_THREONINE-PROTEIN PHOSPHATASE 5 |
| PANTHER Protein Class |
protein phosphatase
protein modifying enzyme |
|
| PANTHER Pathway Category | No pathway information available | |
5 GO annotations of cellular component
| Name | Definition |
|---|---|
| cytoplasm | The contents of a cell excluding the plasma membrane and nucleus, but including other subcellular structures. |
| cytosol | The part of the cytoplasm that does not contain organelles but which does contain other particulate matter, such as protein complexes. |
| mitotic spindle | A spindle that forms as part of mitosis. Mitotic and meiotic spindles contain distinctive complements of proteins associated with microtubules. |
| 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. |
| protein-containing complex | A stable assembly of two or more macromolecules, i.e. proteins, nucleic acids, carbohydrates or lipids, in which at least one component is a protein and the constituent parts function together. |
4 GO annotations of molecular function
| Name | Definition |
|---|---|
| Hsp90 protein binding | Binding to Hsp90 proteins, any of a group of heat shock proteins around 90kDa in size. |
| metal ion binding | Binding to a metal ion. |
| phosphoprotein phosphatase activity | Catalysis of the reaction: a phosphoprotein + H2O = a protein + phosphate. Together with protein kinases, these enzymes control the state of phosphorylation of cellular proteins and thereby provide an important mechanism for regulating cellular activity. |
| protein serine/threonine phosphatase activity | Catalysis of the reaction: protein serine phosphate + H2O = protein serine + phosphate, and protein threonine phosphate + H2O = protein threonine + phosphate. |
2 GO annotations of biological process
| Name | Definition |
|---|---|
| negative regulation of exocytosis | Any process that stops, prevents, or reduces the frequency, rate or extent of exocytosis. |
| protein localization to organelle | A process in which a protein is transported to, or maintained in, a location within an organelle. |
6 homologous proteins in AiPD
| UniProt AC | Gene Name | Protein Name | Species | Evidence Code |
|---|---|---|---|---|
| P53043 | PPT1 | Serine/threonine-protein phosphatase T | Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast) | SS |
| P53041 | PPP5C | Serine/threonine-protein phosphatase 5 | Homo sapiens (Human) | EV |
| Q60676 | Ppp5c | Serine/threonine-protein phosphatase 5 | Mus musculus (Mouse) | SS |
| P53042 | Ppp5c | Serine/threonine-protein phosphatase 5 | Rattus norvegicus (Rat) | EV |
| Q84XU2 | PAPP5 | Serine/threonine-protein phosphatase 5 | Arabidopsis thaliana (Mouse-ear cress) | SS |
| Q84K11 | PP5 | Serine/threonine-protein phosphatase 5 | Solanum lycopersicum (Tomato) (Lycopersicon esculentum) | PR |
| 10 | 20 | 30 | 40 | 50 | 60 |
| MAATITDDIV | ATVLESIEEK | SYEDEKEKAG | MIKDEANQFF | KDQVYDVAAD | LYSVAIEIHP |
| 70 | 80 | 90 | 100 | 110 | 120 |
| TAVLYGNRAQ | AYLKKELYGS | ALEDADNAIA | IDPSYVKGFY | RRATANMALG | RFKKALTDYQ |
| 130 | 140 | 150 | 160 | 170 | 180 |
| AVVKVCPNDK | DARAKFDECS | KIVRRQKFEA | AISTDHDKKT | VAETLDINAM | AIEDSYDGPR |
| 190 | 200 | 210 | 220 | 230 | 240 |
| LEDKITKEFV | LQLIKTFKNQ | QKLHKKYAFK | MLLEFYNYVK | SLPTMVEITV | PTGKKFTICG |
| 250 | 260 | 270 | 280 | 290 | 300 |
| DVHGQFYDLC | NIFEINGYPS | ETNPYLFNGD | FVDRGSFSVE | TIFTMIGFKL | LYPNHFFMSR |
| 310 | 320 | 330 | 340 | 350 | 360 |
| GNHESDVMNK | MYGFEGEVKA | KYTQQMCDMF | TETFCWLPLC | HLINEKIFVC | HGGLFKEDGV |
| 370 | 380 | 390 | 400 | 410 | 420 |
| TLEDIRKTDR | NRQPPDEGIM | CDLLWSDPQP | INGRSPSKRG | VGCQFGPDVT | SKWCETNGIE |
| 430 | 440 | 450 | 460 | 470 | 480 |
| YVVRSHEVKP | EGYEMHHNGQ | CFTVFSAPNY | CDQMNNKGAF | ITITGDNLTP | RFTPFDAVPH |
| 490 | |||||
| PKLPPMAYAN | SLFGFN |