Q8BFW3
PR
Gene name |
Ppp1r15b |
Protein name |
Protein phosphatase 1 regulatory subunit 15B |
Names |
Constitutive repressor of eIF2alpha phosphorylation, CReP |
Species |
Mus musculus (Mouse) |
KEGG Pathway |
mmu:108954 |
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 Q8BFW3
| Entry ID | Method | Resolution | Chain | Position | Source |
|---|---|---|---|---|---|
| AF-Q8BFW3-F1 | Predicted | AlphaFoldDB |
39 variants for Q8BFW3
| Variant ID(s) | Position | Change | Description | Diseaes Association | Provenance |
|---|---|---|---|---|---|
| rs244709538 | 31 | C>S | No | EVA | |
| rs3388498108 | 64 | L>F | No | EVA | |
| rs3388497858 | 82 | F>L | No | EVA | |
| rs3388500629 | 154 | L>I | No | EVA | |
| rs211918659 | 164 | A>P | No | EVA | |
| rs3390619948 | 185 | Q>H | No | EVA | |
| rs33493872 | 202 | L>R | No | EVA | |
| rs218331015 | 204 | V>A | No | EVA | |
| rs3388497580 | 218 | N>K | No | EVA | |
| rs3388499175 | 231 | R>H | No | EVA | |
| rs258672199 | 232 | C>Y | No | EVA | |
| rs3390666050 | 233 | Q>L | No | EVA | |
| rs217272847 | 234 | S>I | No | EVA | |
| rs217272847 | 234 | S>N | No | EVA | |
| rs3390646770 | 234 | S>R | No | EVA | |
| rs3390645218 | 236 | A>P | No | EVA | |
| rs3388499263 | 255 | S>Y | No | EVA | |
| rs33493867 | 277 | P>Q | No | EVA | |
| rs3388497641 | 284 | L>M | No | EVA | |
| rs3388501542 | 294 | R>Q | No | EVA | |
| rs3388497855 | 309 | P>L | No | EVA | |
| rs3390656901 | 317 | S>PEKVMFLLQAMIAIILVRGG* | No | EVA | |
| rs247559018 | 347 | P>L | No | EVA | |
| rs229848174 | 387 | A>V | No | EVA | |
| rs33493063 | 398 | P>S | No | EVA | |
| rs3390666057 | 410 | I>V | No | EVA | |
| rs3388498100 | 469 | D>N | No | EVA | |
| rs266105629 | 488 | P>S | No | EVA | |
| rs234009486 | 502 | C>S | No | EVA | |
| rs257523000 | 510 | G>E | No | EVA | |
| rs33493061 | 528 | P>S | No | EVA | |
| rs212421502 | 544 | H>N | No | EVA | |
| rs231049718 | 550 | N>S | No | EVA | |
| rs252800919 | 560 | P>T | No | EVA | |
| rs227519694 | 572 | K>E | No | EVA | |
| rs237633072 | 592 | A>S | No | EVA | |
| rs3388497505 | 659 | I>F | No | EVA | |
| rs3388498148 | 683 | R>G | No | EVA | |
| rs3388500088 | 694 | N>K | No | EVA |
No associated diseases with Q8BFW3
2 GO annotations of cellular component
| Name | Definition |
|---|---|
| endoplasmic reticulum | The irregular network of unit membranes, visible only by electron microscopy, that occurs in the cytoplasm of many eukaryotic cells. The membranes form a complex meshwork of tubular channels, which are often expanded into slitlike cavities called cisternae. The ER takes two forms, rough (or granular), with ribosomes adhering to the outer surface, and smooth (with no ribosomes attached). |
| protein phosphatase type 1 complex | A protein complex that possesses magnesium-dependent protein serine/threonine phosphatase (AMD phosphatase) activity, and consists of a catalytic subunit and one or more regulatory subunits that dictates the phosphatase's substrate specificity, function, and activity. |
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. |
9 GO annotations of biological process
| Name | Definition |
|---|---|
| ER overload response | The series of molecular signals initiated by the accumulation of normal or misfolded proteins in the endoplasmic reticulum and leading to activation of transcription by NF-kappaB. |
| negative regulation of endoplasmic reticulum stress-induced eIF2 alpha phosphorylation | Any process that stops, prevents or reduces the frequency, rate or extent of endoplasmic reticulum stress-induced eiF2alpha phosphorylation. |
| negative regulation of protein phosphorylation | Any process that stops, prevents or reduces the rate of addition of phosphate groups to amino acids within a protein. |
| peptidyl-serine dephosphorylation | The removal of phosphoric residues from peptidyl-O-phospho-L-serine to form peptidyl-serine. |
| positive regulation of phosphoprotein phosphatase activity | Any process that activates or increases the activity of a phosphoprotein phosphatase. |
| regulation of translational initiation | Any process that modulates the frequency, rate or extent of translational initiation. |
| response to endoplasmic reticulum stress | Any process that results in a change in state or activity of a cell (in terms of movement, secretion, enzyme production, gene expression, etc.) as a result of a stress acting at the endoplasmic reticulum. ER stress usually results from the accumulation of unfolded or misfolded proteins in the ER lumen. |
| response to hydrogen peroxide | Any process that results in a change in state or activity of a cell or an organism (in terms of movement, secretion, enzyme production, gene expression, etc.) as a result of a hydrogen peroxide (H2O2) stimulus. |
| response to oxidative stress | Any process that results in a change in state or activity of a cell or an organism (in terms of movement, secretion, enzyme production, gene expression, etc.) as a result of oxidative stress, a state often resulting from exposure to high levels of reactive oxygen species, e.g. superoxide anions, hydrogen peroxide (H2O2), and hydroxyl radicals. |
1 homologous proteins in AiPD
| UniProt AC | Gene Name | Protein Name | Species | Evidence Code |
|---|---|---|---|---|
| Q5SWA1 | PPP1R15B | Protein phosphatase 1 regulatory subunit 15B | Homo sapiens (Human) | PR |
| 10 | 20 | 30 | 40 | 50 | 60 |
| METGTHRARK | RPGPRLGSWF | RLPFLRRSHA | CSSEFPPPSS | RQNPGNSALP | ERRTRYWTKL |
| 70 | 80 | 90 | 100 | 110 | 120 |
| LSQLLALLPS | LFQKLLLWSQ | LFGGLIPTRW | LDFAASYSAL | RALRGREESA | APTVQKSLSS |
| 130 | 140 | 150 | 160 | 170 | 180 |
| LRLDSSEDLV | VSSLDWLEEG | LQWQCSSSDL | ELKLKAQERA | LDSAAPTFLL | EQQLWGVELL |
| 190 | 200 | 210 | 220 | 230 | 240 |
| PSSLQAGLVS | HRELDSSSSG | PLSVQSLGNF | KVVSYLLNPS | YLDYLPQLGL | RCQSSAGGGQ |
| 250 | 260 | 270 | 280 | 290 | 300 |
| FVGFRTLTPE | SCYLSEDGCH | PQPLRAEMSA | TAWRRCPPLS | TEGLPEIHHL | RMKRLEFLQA |
| 310 | 320 | 330 | 340 | 350 | 360 |
| NKGQELPTPD | QDNGYHSLEE | EHNLLRMDPQ | HCTDNPAQAV | SPAADRPEPT | EKKPELVIQE |
| 370 | 380 | 390 | 400 | 410 | 420 |
| VSQSPQGSSL | FCELPVEKEC | EEDHTNATDL | SDRGESLPVS | TRPVCSNKLI | DYILGGAPSD |
| 430 | 440 | 450 | 460 | 470 | 480 |
| LEASSDSESE | DWGEEPEDDG | FDSDGSLSES | DVEQDSEGLH | LWNSFHSVDP | YNPQNFTATI |
| 490 | 500 | 510 | 520 | 530 | 540 |
| QTAARIAPRD | PSDSGTSWSG | SCGVGSCQEG | PLPETPDHSS | GEEDDWEPSA | DEAENLKLWN |
| 550 | 560 | 570 | 580 | 590 | 600 |
| SFCHSEDPYN | LLNFKAPFQP | SGKNWKGRQD | SKASSEATVA | FSGHHTLLSC | KAQLLESQED |
| 610 | 620 | 630 | 640 | 650 | 660 |
| NCPGCGLGEA | LAGERYTHIK | RKKVTFLEEV | TEYYISGDED | RKGPWEEFAR | DGCRFQKRIQ |
| 670 | 680 | 690 | |||
| ETEVAIGYCL | AFEHREKMFN | RLRIESKDLL | LYSNVKK |