Q6PD03
PR
Gene name |
Ppp2r5a |
Protein name |
Serine/threonine-protein phosphatase 2A 56 kDa regulatory subunit alpha isoform |
Names |
PP2A B subunit isoform B'-alpha, PP2A B subunit isoform B56-alpha, PP2A B subunit isoform PR61-alpha, PR61alpha, PP2A B subunit isoform R5-alpha |
Species |
Mus musculus (Mouse) |
KEGG Pathway |
mmu:226849 |
EC number |
|
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 Q6PD03
| Entry ID | Method | Resolution | Chain | Position | Source |
|---|---|---|---|---|---|
| AF-Q6PD03-F1 | Predicted | AlphaFoldDB |
11 variants for Q6PD03
| Variant ID(s) | Position | Change | Description | Diseaes Association | Provenance |
|---|---|---|---|---|---|
| rs3388522673 | 97 | K>R | No | EVA | |
| rs3388522733 | 117 | E>D | No | EVA | |
| rs3388524597 | 155 | S>Y | No | EVA | |
| rs1135123220 | 225 | I>T | No | EVA | |
| rs33841959 | 228 | Q>H | No | EVA | |
| rs3388526910 | 252 | I>V | No | EVA | |
| rs3388524660 | 301 | E>* | No | EVA | |
| rs3388523110 | 305 | T>M | No | EVA | |
| rs3388527585 | 346 | K>R | No | EVA | |
| rs3388523176 | 374 | F>L | No | EVA | |
| rs3388524553 | 380 | I>T | No | EVA |
No associated diseases with Q6PD03
No regional properties for Q6PD03
| Type | Name | Position | InterPro Accession |
|---|---|---|---|
| No domain, repeats, and functional sites for Q6PD03 | |||
Functions
9 GO annotations of cellular component
| Name | Definition |
|---|---|
| centrosome | A structure comprised of a core structure (in most organisms, a pair of centrioles) and peripheral material from which a microtubule-based structure, such as a spindle apparatus, is organized. Centrosomes occur close to the nucleus during interphase in many eukaryotic cells, though in animal cells it changes continually during the cell-division cycle. |
| chromosome, centromeric region | The region of a chromosome that includes the centromeric DNA and associated proteins. In monocentric chromosomes, this region corresponds to a single area of the chromosome, whereas in holocentric chromosomes, it is evenly distributed along the chromosome. |
| 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. |
| M band | The midline of aligned thick filaments in a sarcomere; location of specific proteins that link thick filaments. Depending on muscle type the M band consists of different numbers of M lines. |
| membrane | A lipid bilayer along with all the proteins and protein complexes embedded in it an attached to it. |
| 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. |
| Z disc | Platelike region of a muscle sarcomere to which the plus ends of actin filaments are attached. |
3 GO annotations of molecular function
| Name | Definition |
|---|---|
| kinase binding | Binding to a kinase, any enzyme that catalyzes the transfer of a phosphate group. |
| 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 phosphatase activator activity | Binds to and increases the activity of a protein phosphatase, an enzyme which catalyzes of the removal of a phosphate group from a protein substrate molecule. |
5 GO annotations of biological process
| Name | Definition |
|---|---|
| negative regulation of lipid kinase activity | Any process that decreases the frequency, rate or extent of lipid kinase activity, the catalysis of the transfer of a phosphate group, usually from ATP, to a simple or complex lipid. |
| negative regulation of protein localization to plasma membrane | Any process that stops, prevents or reduces the frequency, rate or extent of protein localization to plasma membrane. |
| positive regulation of protein dephosphorylation | Any process that activates or increases the frequency, rate or extent of removal of phosphate groups from a protein. |
| protein dephosphorylation | The process of removing one or more phosphoric residues from a protein. |
| signal transduction | The cellular process in which a signal is conveyed to trigger a change in the activity or state of a cell. Signal transduction begins with reception of a signal (e.g. a ligand binding to a receptor or receptor activation by a stimulus such as light), or for signal transduction in the absence of ligand, signal-withdrawal or the activity of a constitutively active receptor. Signal transduction ends with regulation of a downstream cellular process, e.g. regulation of transcription or regulation of a metabolic process. Signal transduction covers signaling from receptors located on the surface of the cell and signaling via molecules located within the cell. For signaling between cells, signal transduction is restricted to events at and within the receiving cell. |
13 homologous proteins in AiPD
| UniProt AC | Gene Name | Protein Name | Species | Evidence Code |
|---|---|---|---|---|
| A4FV68 | PPP2R5E | Serine/threonine-protein phosphatase 2A 56 kDa regulatory subunit epsilon isoform | Bos taurus (Bovine) | PR |
| Q15173 | PPP2R5B | Serine/threonine-protein phosphatase 2A 56 kDa regulatory subunit beta isoform | Homo sapiens (Human) | PR |
| Q16537 | PPP2R5E | Serine/threonine-protein phosphatase 2A 56 kDa regulatory subunit epsilon isoform | Homo sapiens (Human) | PR |
| Q14738 | PPP2R5D | Serine/threonine-protein phosphatase 2A 56 kDa regulatory subunit delta isoform | Homo sapiens (Human) | PR |
| Q15172 | PPP2R5A | Serine/threonine-protein phosphatase 2A 56 kDa regulatory subunit alpha isoform | Homo sapiens (Human) | PR |
| Q61151 | Ppp2r5e | Serine/threonine-protein phosphatase 2A 56 kDa regulatory subunit epsilon isoform | Mus musculus (Mouse) | PR |
| O04375 | B'ALPHA | Serine/threonine protein phosphatase 2A 57 kDa regulatory subunit B' alpha isoform | Arabidopsis thaliana (Mouse-ear cress) | PR |
| Q8LF36 | B'THETA | Serine/threonine protein phosphatase 2A 57 kDa regulatory subunit B' theta isoform | Arabidopsis thaliana (Mouse-ear cress) | PR |
| Q8RW96 | B'GAMMA | Serine/threonine protein phosphatase 2A 59 kDa regulatory subunit B' gamma isoform | Arabidopsis thaliana (Mouse-ear cress) | PR |
| Q93YV6 | B'KAPPA | Serine/threonine protein phosphatase 2A 57 kDa regulatory subunit B' kappa isoform | Arabidopsis thaliana (Mouse-ear cress) | PR |
| Q9LVE2 | B'ZETA | Serine/threonine protein phosphatase 2A 59 kDa regulatory subunit B' zeta isoform | Arabidopsis thaliana (Mouse-ear cress) | PR |
| Q9ZQY6 | B'DELTA | Serine/threonine protein phosphatase 2A 55 kDa regulatory subunit B' delta isoform | Arabidopsis thaliana (Mouse-ear cress) | PR |
| Q9LU89 | B'ETA | Serine/threonine protein phosphatase 2A 59 kDa regulatory subunit B' eta isoform | Arabidopsis thaliana (Mouse-ear cress) | PR |
| 10 | 20 | 30 | 40 | 50 | 60 |
| MSSPSPPAPV | ACAAISASEK | VDGFTRKSVR | KAQRQKRSQG | SSQFRSQGSQ | AELHPLPQLK |
| 70 | 80 | 90 | 100 | 110 | 120 |
| DATSNEQQEL | FCQKLQQCCV | LFDFMDSVSD | LKSKEIKRAT | LNELVEYVST | NRGVIVESAY |
| 130 | 140 | 150 | 160 | 170 | 180 |
| SDIVKMISAN | IFRTLPPSDN | PDFDPEEDEP | TLEASWPHIQ | LVYEFFLRFL | ESPDFQPSIA |
| 190 | 200 | 210 | 220 | 230 | 240 |
| KRYIDQKFVQ | QLLELFDSED | PRERDFLKTV | LHRIYGKFLG | LRAFIRKQIN | NIFLRFIYET |
| 250 | 260 | 270 | 280 | 290 | 300 |
| EHFNGVAELL | EILGSIINGF | ALPLKAEHKQ | FLMKVLIPMH | TAKGLALFHA | QLAYCVVQFL |
| 310 | 320 | 330 | 340 | 350 | 360 |
| EKDTTLTEPV | IRGLLKFWPK | TCSQKEVMFL | GEIEEILDVI | EPTQFKKIEE | PLFKQISKCV |
| 370 | 380 | 390 | 400 | 410 | 420 |
| SSSHFQVAER | ALYFWNNEYI | LSLIEENIDK | ILPIMFASLY | KISKEHWNQT | IVALVYNVLK |
| 430 | 440 | 450 | 460 | 470 | 480 |
| TLMEMNGKLF | DDLTSSYKAE | RQREKKKELE | REELWKKLEE | LQLKKALEKQ | NNAYNMHSIR |
| SSTSAK |