P53043
SS
Gene name |
PPT1 (YGR123C, G6347) |
Protein name |
Serine/threonine-protein phosphatase T |
Names |
PPT , EC 3.1.3.16 |
Species |
Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast) |
KEGG Pathway |
sce:YGR123C |
EC number |
3.1.3.16: Phosphoric monoester hydrolases |
Protein Class |
|
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 |
142-513 (Phosphatase domain) |
Relief mechanism |
Partner binding |
Assay |
|
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
- Kang H et al. (2001) "Identification of amino acids in the tetratricopeptide repeat and C-terminal domains of protein phosphatase 5 involved in autoinhibition and lipid activation", Biochemistry, 40, 10485-90
- Oberoi J et al. (2016) "Structural and functional basis of protein phosphatase 5 substrate specificity", Proceedings of the National Academy of Sciences of the United States of America, 113, 9009-14
- Cliff MJ et al. (2006) "Conformational diversity in the TPR domain-mediated interaction of protein phosphatase 5 with Hsp90", Structure (London, England : 1993), 14, 415-26
Autoinhibited structure
Activated structure
2 structures for P53043
| Entry ID | Method | Resolution | Chain | Position | Source |
|---|---|---|---|---|---|
| 3ICF | X-ray | 230 A | A/B | 179-513 | PDB |
| AF-P53043-F1 | Predicted | AlphaFoldDB |
6 variants for P53043
| Variant ID(s) | Position | Change | Description | Diseaes Association | Provenance |
|---|---|---|---|---|---|
| s07-738009 | 67 | N>I | No | SGRP | |
| s07-737880 | 110 | K>R | No | SGRP | |
| s07-737541 | 223 | T>I | No | SGRP | |
| s07-737506 | 235 | E>K | No | SGRP | |
| s07-737486 | 241 | D>E | No | SGRP | |
| s07-737194 | 339 | A>S | No | SGRP |
No associated diseases with P53043
7 regional properties for P53043
| Type | Name | Position | InterPro Accession |
|---|---|---|---|
| domain | Calcineurin-like phosphoesterase domain, ApaH type | 243 - 436 | IPR004843 |
| domain | Serine/threonine-specific protein phosphatase/bis(5-nucleosyl)-tetraphosphatase | 209 - 497 | IPR006186 |
| domain | PPP domain | 122 - 233 | IPR013235 |
| repeat | Tetratricopeptide repeat | 12 - 45 | IPR019734-1 |
| repeat | Tetratricopeptide repeat | 46 - 79 | IPR019734-2 |
| repeat | Tetratricopeptide repeat | 80 - 113 | IPR019734-3 |
| domain | PP5, C-terminal metallophosphatase domain | 165 - 508 | IPR041753 |
Functions
| Description | ||
|---|---|---|
| EC Number | 3.1.3.16 | Phosphoric monoester hydrolases |
| Subcellular Localization |
|
|
| PANTHER Family | ||
| PANTHER Subfamily | ||
| PANTHER Protein Class | ||
| PANTHER Pathway Category | No pathway information available | |
3 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. |
| 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. |
3 GO annotations of molecular function
| Name | Definition |
|---|---|
| metal ion binding | Binding to a metal ion. |
| myosin phosphatase activity | Catalysis of the reaction |
| protein serine/threonine phosphatase activity | Catalysis of the reaction |
1 GO annotations of biological process
| Name | Definition |
|---|---|
| protein dephosphorylation | The process of removing one or more phosphoric residues from a protein. |
6 homologous proteins in AiPD
| UniProt AC | Gene Name | Protein Name | Species | Evidence Code |
|---|---|---|---|---|
| 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 |
| Q9NES8 | pph-5 | Serine/threonine-protein phosphatase 5 | Caenorhabditis elegans | 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 |
| MSTPTAADRA | KALERKNEGN | VFVKEKHFLK | AIEKYTEAID | LDSTQSIYFS | NRAFAHFKVD |
| 70 | 80 | 90 | 100 | 110 | 120 |
| NFQSALNDCD | EAIKLDPKNI | KAYHRRALSC | MALLEFKKAR | KDLNVLLKAK | PNDPAATKAL |
| 130 | 140 | 150 | 160 | 170 | 180 |
| LTCDRFIREE | RFRKAIGGAE | NEAKISLCQT | LNLSSFDANA | DLANYEGPKL | EFEQLYDDKN |
| 190 | 200 | 210 | 220 | 230 | 240 |
| AFKGAKIKNM | SQEFISKMVN | DLFLKGKYLP | KKYVAAIISH | ADTLFRQEPS | MVELENNSTP |
| 250 | 260 | 270 | 280 | 290 | 300 |
| DVKISVCGDT | HGQFYDVLNL | FRKFGKVGPK | HTYLFNGDFV | DRGSWSCEVA | LLFYCLKILH |
| 310 | 320 | 330 | 340 | 350 | 360 |
| PNNFFLNRGN | HESDNMNKIY | GFEDECKYKY | SQRIFNMFAQ | SFESLPLATL | INNDYLVMHG |
| 370 | 380 | 390 | 400 | 410 | 420 |
| GLPSDPSATL | SDFKNIDRFA | QPPRDGAFME | LLWADPQEAN | GMGPSQRGLG | HAFGPDITDR |
| 430 | 440 | 450 | 460 | 470 | 480 |
| FLRNNKLRKI | FRSHELRMGG | VQFEQKGKLM | TVFSAPNYCD | SQGNLGGVIH | VVPGHGILQA |
| 490 | 500 | 510 | |||
| GRNDDQNLII | ETFEAVEHPD | IKPMAYSNGG | FGL |