P58389
PR
Gene name |
Ptpa (Ppp2r4) |
Protein name |
Serine/threonine-protein phosphatase 2A activator |
Names |
PP2A, subunit B', PR53 isoform, Phosphotyrosyl phosphatase activator, PTPA, Serine/threonine-protein phosphatase 2A regulatory subunit 4, Serine/threonine-protein phosphatase 2A regulatory subunit B' |
Species |
Mus musculus (Mouse) |
KEGG Pathway |
mmu:110854 |
EC number |
5.2.1.8: Cis-trans isomerases |
Protein Class |
|
Descriptions
The autoinhibited protein was predicted that may have potential autoinhibitory elements via cis-regPred.
Autoinhibitory domains (AIDs)
Target domain |
|
Relief mechanism |
|
Assay |
cis-regPred |
Accessory elements
No accessory elements
Autoinhibited structure
Activated structure
1 structures for P58389
| Entry ID | Method | Resolution | Chain | Position | Source |
|---|---|---|---|---|---|
| AF-P58389-F1 | Predicted | AlphaFoldDB |
13 variants for P58389
| Variant ID(s) | Position | Change | Description | Diseaes Association | Provenance |
|---|---|---|---|---|---|
| rs27193572 | 19 | T>A | No | EVA | |
| rs3388543180 | 25 | I>V | No | EVA | |
| rs3388538117 | 28 | K>N | No | EVA | |
| rs3388538097 | 29 | E>K | No | EVA | |
| rs3388539326 | 30 | I>L | No | EVA | |
| rs3388544997 | 69 | K>N | No | EVA | |
| rs3388537071 | 113 | D>V | No | EVA | |
| rs3413120459 | 116 | A>T | No | EVA | |
| rs3388537064 | 156 | E>K | No | EVA | |
| rs3388542414 | 159 | F>Y | No | EVA | |
| rs3388536424 | 177 | Q>L | No | EVA | |
| rs3388536441 | 267 | P>L | No | EVA | |
| rs3388540780 | 301 | E>A | No | EVA |
No associated diseases with P58389
No regional properties for P58389
| Type | Name | Position | InterPro Accession |
|---|---|---|---|
| No domain, repeats, and functional sites for P58389 | |||
Functions
| Description | ||
|---|---|---|
| EC Number | 5.2.1.8 | Cis-trans isomerases |
| Subcellular Localization |
|
|
| PANTHER Family | ||
| PANTHER Subfamily | ||
| PANTHER Protein Class | ||
| PANTHER Pathway Category | No pathway information available | |
6 GO annotations of cellular component
| Name | Definition |
|---|---|
| ATPase complex | A protein complex which is capable of ATPase activity. |
| calcium channel complex | An ion channel complex through which calcium ions pass. |
| cytoplasm | The contents of a cell excluding the plasma membrane and nucleus, but including other subcellular structures. |
| nucleoplasm | That part of the nuclear content other than the chromosomes or the nucleolus. |
| 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 phosphatase type 2A complex | A protein complex that has protein serine/threonine phosphatase activity that is polycation-stimulated (PCS), being directly stimulated by protamine, polylysine, or histone H1; it constitutes a subclass of several enzymes activated by different histones and polylysine, and consists of catalytic, scaffolding, and regulatory subunits. The catalytic and scaffolding subunits form the core enzyme, and the holoenzyme also includes the regulatory subunit. |
8 GO annotations of molecular function
| Name | Definition |
|---|---|
| ATP binding | Binding to ATP, adenosine 5'-triphosphate, a universally important coenzyme and enzyme regulator. |
| peptidyl-prolyl cis-trans isomerase activity | Catalysis of the reaction: peptidyl-proline (omega=180) = peptidyl-proline (omega=0). |
| 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 homodimerization activity | Binding to an identical protein to form a homodimer. |
| protein phosphatase 2A binding | Binding to protein phosphatase 2A. |
| protein phosphatase regulator activity | Binds to and modulates the activity of a protein phosphatase, an enzyme which catalyzes of the removal of a phosphate group from a protein substrate molecule. |
| protein tyrosine phosphatase activator activity | Binds to and increases the activity of a phosphatase, an enzyme which catalyzes of the removal of a phosphate group from a tyrosyl phenolic group of a protein. |
| signaling receptor binding | Binding to one or more specific sites on a receptor molecule, a macromolecule that undergoes combination with a hormone, neurotransmitter, drug or intracellular messenger to initiate a change in cell function. |
7 GO annotations of biological process
| Name | Definition |
|---|---|
| mitotic spindle organization | A process that is carried out at the cellular level which results in the assembly, arrangement of constituent parts, or disassembly of the microtubule spindle during a mitotic cell cycle. |
| negative regulation of phosphoprotein phosphatase activity | Any process that stops or reduces the activity of a phosphoprotein phosphatase. |
| negative regulation of protein dephosphorylation | Any process the stops, prevents, or reduces the frequency, rate or extent of removal of phosphate groups from a protein. |
| positive regulation of apoptotic process | Any process that activates or increases the frequency, rate or extent of cell death by apoptotic process. |
| positive regulation of phosphoprotein phosphatase activity | Any process that activates or increases the activity of a phosphoprotein phosphatase. |
| positive regulation of protein dephosphorylation | Any process that activates or increases the frequency, rate or extent of removal of phosphate groups from a protein. |
| regulation of phosphoprotein phosphatase activity | Any process that modulates the frequency, rate or extent of phosphoprotein phosphatase activity, the catalysis of the hydrolysis of phosphate from a phosphoprotein. |
No homologous proteins in AiPD
| UniProt AC | Gene Name | Protein Name | Species | Evidence Code |
|---|---|---|---|---|
| No homologous proteins | ||||
| 10 | 20 | 30 | 40 | 50 | 60 |
| MAEGERQPPP | DSSEETPPTT | QNFIIPKKEI | HTVPDMGKWK | RSQAYADYIG | FILTLNEGVK |
| 70 | 80 | 90 | 100 | 110 | 120 |
| GKKLTFDYKV | SEAIEKLVAL | LDTLDRWIDE | TPPVDQPSRF | GNKAYRTWYA | KLDQEAENLV |
| 130 | 140 | 150 | 160 | 170 | 180 |
| ATVVPTHLAA | AVPEVAVYLK | EAVGNSTRID | YGTGHEAAFA | AFLCCLCKIG | VLRVDDQVAI |
| 190 | 200 | 210 | 220 | 230 | 240 |
| VFKVFDRYLE | VMRKLQKTYR | MEPAGSQGVW | GLDDFQFLPF | IWGSSQLIDH | PHLEPRHFVD |
| 250 | 260 | 270 | 280 | 290 | 300 |
| EKAVSENHKD | YMFLQCILFI | TEMKTGPFAE | HSNQLWNISA | VPSWSKVNQG | LIRMYKAECL |
| 310 | 320 | ||||
| EKFPVIQHFK | FGSLLPIHPV | TSG |