A1L3L9
Gene name |
ppp2r2b (ppp2r2b-a, ppp2r2c) |
Protein name |
Serine/threonine-protein phosphatase 2A 55 kDa regulatory subunit B beta isoform |
Names |
PP2A subunit B isoform B55-beta, PP2A subunit B isoform PR55-beta, PP2A subunit B isoform R2-beta, PP2A subunit B isoform beta |
Species |
Xenopus laevis (African clawed frog) |
KEGG Pathway |
xla:394301 |
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 A1L3L9
| Entry ID | Method | Resolution | Chain | Position | Source |
|---|---|---|---|---|---|
| AF-A1L3L9-F1 | Predicted | AlphaFoldDB |
No variants for A1L3L9
| Variant ID(s) | Position | Change | Description | Diseaes Association | Provenance |
|---|---|---|---|---|---|
| No variants for A1L3L9 | |||||
No associated diseases with A1L3L9
8 regional properties for A1L3L9
| Type | Name | Position | InterPro Accession |
|---|---|---|---|
| repeat | WD40 repeat | 38 - 77 | IPR001680-1 |
| repeat | WD40 repeat | 104 - 144 | IPR001680-2 |
| repeat | WD40 repeat | 186 - 225 | IPR001680-3 |
| repeat | WD40 repeat | 239 - 276 | IPR001680-4 |
| repeat | WD40 repeat | 295 - 333 | IPR001680-5 |
| repeat | WD40 repeat | 427 - 464 | IPR001680-6 |
| conserved_site | Protein phosphatase 2A regulatory subunit PR55, conserved site | 104 - 118 | IPR018067-1 |
| conserved_site | Protein phosphatase 2A regulatory subunit PR55, conserved site | 195 - 209 | IPR018067-2 |
4 GO annotations of cellular component
| Name | Definition |
|---|---|
| cytoplasm | The contents of a cell excluding the plasma membrane and nucleus, but including other subcellular structures. |
| cytoskeleton | A cellular structure that forms the internal framework of eukaryotic and prokaryotic cells. The cytoskeleton includes intermediate filaments, microfilaments, microtubules, the microtrabecular lattice, and other structures characterized by a polymeric filamentous nature and long-range order within the cell. The various elements of the cytoskeleton not only serve in the maintenance of cellular shape but also have roles in other cellular functions, including cellular movement, cell division, endocytosis, and movement of organelles. |
| membrane | A lipid bilayer along with all the proteins and protein complexes embedded in it an attached to it. |
| 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. |
1 GO annotations of molecular function
| Name | Definition |
|---|---|
| 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. |
No GO annotations of biological process
| Name | Definition |
|---|---|
| No GO annotations for biological process |
No homologous proteins in AiPD
| UniProt AC | Gene Name | Protein Name | Species | Evidence Code |
|---|---|---|---|---|
| No homologous proteins | ||||
| 10 | 20 | 30 | 40 | 50 | 60 |
| MPCSVEDKTG | LCGSRYSVMI | PELQESVIFS | EDSRHYNEKQ | TRRQRKSSAD | IISTVEFNNT |
| 70 | 80 | 90 | 100 | 110 | 120 |
| GELLATGDKG | GRVVIFQREQ | ENKNQPHRRG | EYNVYSTFQS | HEPEFDYLKS | LEIEEKINKI |
| 130 | 140 | 150 | 160 | 170 | 180 |
| RWLPQQNAAY | FLLSTNDKTV | KLWKVSERDK | RPEGYNLKDE | EGRIRDPCTI | TSLRVPVLRP |
| 190 | 200 | 210 | 220 | 230 | 240 |
| MDLMVEATPR | RVFSNAHTYH | INSISVNSDY | ETYMSADDLR | INLWNLEITN | RSFNIVDIKP |
| 250 | 260 | 270 | 280 | 290 | 300 |
| TNMEELTEVI | TAAEFHPHNC | NTFVYSSSKG | TIRLCDMRSS | ALCDKHSKLF | EEPEDPSNRS |
| 310 | 320 | 330 | 340 | 350 | 360 |
| FFSEIISSIS | DVKFNHSGRY | IMTRDYLTVK | VWDLNMENRP | IETYQVHDYL | RSKLCSLYEN |
| 370 | 380 | 390 | 400 | 410 | 420 |
| DCIFDKFECV | WNGSDSVIMT | GSYNNFFRMF | DRNTKRDVTL | EASRENSKPR | AILKPRKVCV |
| 430 | 440 | 450 | 460 | ||
| GGKRRKDEIS | VDSLDFSKKI | LHTAWHPSEN | IIAVAATNNL | YIFQDKVN |