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
5 structures for Q5SWA1
| Entry ID | Method | Resolution | Chain | Position | Source |
|---|---|---|---|---|---|
| 4V0U | X-ray | 788 A | E/G/I/K/O | 631-701 | PDB |
| 4V0V | X-ray | 161 A | B/D | 631-660 | PDB |
| 4V0W | X-ray | 155 A | B/D | 631-669 | PDB |
| 4V0X | X-ray | 185 A | B | 631-684 | PDB |
| AF-Q5SWA1-F1 | Predicted | AlphaFoldDB |
7 variants for Q5SWA1
| Variant ID(s) | Position | Change | Description | Diseaes Association | Provenance |
|---|---|---|---|---|---|
|
VAR_074072 rs869025335 RCV000207486 CA351642 |
658 | R>C | Microcephaly, short stature, and impaired glucose metabolism 2 MSSGM2; no effect on localization; increased protein abundance; loss of interaction with protein phosphatase catalytic subunit PP1; decreased dephosphorylation of EIF2S1 [ClinVar, UniProt] | Yes |
ClinGen ClinVar UniProt Ensembl dbSNP |
|
RCV000908469 rs12094135 CA1346912 VAR_039196 |
26 | P>S | No |
ClinGen ClinVar UniProt 1000Genomes ESP ExAC TOPMed dbSNP gnomAD |
|
|
rs755194116 CA1346822 VAR_079851 |
134 | P>S | found in a patient with isolated coloboma; unknown pathological significance [UniProt] | No |
ClinGen UniProt ExAC TOPMed dbSNP gnomAD |
|
RCV001819071 RCV000966777 VAR_039197 CA1346815 rs4492688 |
144 | E>K | No |
ClinGen ClinVar UniProt 1000Genomes ExAC TOPMed dbSNP gnomAD |
|
|
RCV000955277 VAR_039198 CA35772712 rs3014626 |
308 | N>N | No |
ClinGen ClinVar UniProt 1000Genomes ESP ExAC TOPMed dbSNP gnomAD |
|
|
rs2089891 VAR_039199 CA1346688 |
363 | E>G | No |
ClinGen UniProt 1000Genomes ESP ExAC TOPMed dbSNP gnomAD |
|
|
rs17855962 CA1346573 VAR_039200 |
589 | K>E | No |
ClinGen UniProt 1000Genomes ESP ExAC TOPMed dbSNP gnomAD |
2 associated diseases with Q5SWA1
[MIM: 616817]: Microcephaly, short stature, and impaired glucose metabolism 2 (MSSGM2)
An autosomal recessive disease characterized by microcephaly, intellectual disability, short stature, and disturbed glucose metabolism. {ECO:0000269|PubMed:26159176, ECO:0000269|PubMed:26307080}. Note=The disease is caused by variants affecting the gene represented in this entry.
Without disease ID
- An autosomal recessive disease characterized by microcephaly, intellectual disability, short stature, and disturbed glucose metabolism. {ECO:0000269|PubMed:26159176, ECO:0000269|PubMed:26307080}. Note=The disease is caused by variants affecting the gene represented in this entry.
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. |
8 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 PERK-mediated unfolded protein response | Any process that stops, prevents or reduces the frequency, rate or extent of the PERK-mediated unfolded protein response. |
| 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. |
| 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. |
1 homologous proteins in AiPD
| UniProt AC | Gene Name | Protein Name | Species | Evidence Code |
|---|---|---|---|---|
| Q8BFW3 | Ppp1r15b | Protein phosphatase 1 regulatory subunit 15B | Mus musculus (Mouse) | PR |
| 10 | 20 | 30 | 40 | 50 | 60 |
| MEPGTGGSRK | RLGPRAGFRF | WPPFFPRRSQ | AGSSKFPTPL | GPENSGNPTL | LSSAQPETRV |
| 70 | 80 | 90 | 100 | 110 | 120 |
| SYWTKLLSQL | LAPLPGLLQK | VLIWSQLFGG | MFPTRWLDFA | GVYSALRALK | GREKPAAPTA |
| 130 | 140 | 150 | 160 | 170 | 180 |
| QKSLSSLQLD | SSDPSVTSPL | DWLEEGIHWQ | YSPPDLKLEL | KAKGSALDPA | AQAFLLEQQL |
| 190 | 200 | 210 | 220 | 230 | 240 |
| WGVELLPSSL | QSRLYSNREL | GSSPSGPLNI | QRIDNFSVVS | YLLNPSYLDC | FPRLEVSYQN |
| 250 | 260 | 270 | 280 | 290 | 300 |
| SDGNSEVVGF | QTLTPESSCL | REDHCHPQPL | SAELIPASWQ | GCPPLSTEGL | PEIHHLRMKR |
| 310 | 320 | 330 | 340 | 350 | 360 |
| LEFLQQANKG | QDLPTPDQDN | GYHSLEEEHS | LLRMDPKHCR | DNPTQFVPAA | GDIPGNTQES |
| 370 | 380 | 390 | 400 | 410 | 420 |
| TEEKIELLTT | EVPLALEEES | PSEGCPSSEI | PMEKEPGEGR | ISVVDYSYLE | GDLPISARPA |
| 430 | 440 | 450 | 460 | 470 | 480 |
| CSNKLIDYIL | GGASSDLETS | SDPEGEDWDE | EAEDDGFDSD | SSLSDSDLEQ | DPEGLHLWNS |
| 490 | 500 | 510 | 520 | 530 | 540 |
| FCSVDPYNPQ | NFTATIQTAA | RIVPEEPSDS | EKDLSGKSDL | ENSSQSGSLP | ETPEHSSGEE |
| 550 | 560 | 570 | 580 | 590 | 600 |
| DDWESSADEA | ESLKLWNSFC | NSDDPYNPLN | FKAPFQTSGE | NEKGCRDSKT | PSESIVAISE |
| 610 | 620 | 630 | 640 | 650 | 660 |
| CHTLLSCKVQ | LLGSQESECP | DSVQRDVLSG | GRHTHVKRKK | VTFLEEVTEY | YISGDEDRKG |
| 670 | 680 | 690 | 700 | 710 | |
| PWEEFARDGC | RFQKRIQETE | DAIGYCLTFE | HRERMFNRLQ | GTCFKGLNVL | KQC |