Protein:RGS8 |
Protein Summary |
 Gene summary |
| Gene name: RGS8 | ASpdb.0 ID: 85397 | Gene | Gene symbol | RGS8 | Gene ID | 85397 |
| Gene name | regulator of G protein signaling 8 |
| Synonyms | - |
| Cytomap | 1q25.3 |
| Type of gene | protein-coding |
| Description | regulator of G-protein signaling 8regulator of G-protein signalling 8 |
| Modification date | 20240305 |
| UniProtAcc | P57771 |
| Gene ontology of this gene with evidence of Inferred from Direct Assay (IDA) from Entrez |
| Partner | Gene | GO ID | GO term | PubMed ID |
| Gene | RGS8 | GO:0005096 | GTPase activator activity | 18434541 |
| Gene | RGS8 | GO:0043547 | positive regulation of GTPase activity | 18434541 |
AS Summary |
| Information of the canonical protein with experimentally identified structure from PDB (2023). |
| UniProt Acc | File name | PDB ID | Method | Resolution | Chain | Start | End |
| P57771-1 | P57771-1_5do9_B.pdb | 5DO9 | X-ray | 2.6 | B | 42 | 173 |
| ASpdb's canonical and alternatively spliced isoform information. |
| accession_id | gene_name | canonical_id | alternative_id | canonical_length | alternative_length | canonical_start | canonical_end | type | originalSEQ | variationSEQ | alternative_start | alternative_end |
| P57771 | RGS8 | P57771-1 | P57771-2 | 180 | 198 | 1 | 9 | Substitution | MAALLMPRR | MWNTLTRSLSDHPVGKDPQAMRTGQRQ | 1 | 27 |
| Multiple sequence alignment of our canonical and alternatively spliced RGS8 |
| Matched gene isoform IDs with Ensembl and RefSeq of our canonical and alternative spliced genes of RGS8 |
| UniProt-id | ENSG | ENST | ENSP |
| P57771-1 | ENSG00000135824.13 | ENST00000367556.5 | ENSP00000356527.1 |
| P57771-1 | ENSG00000135824.13 | ENST00000367557.8 | ENSP00000356528.4 |
| P57771-1 | ENSG00000135824.13 | ENST00000483095.6 | ENSP00000426289.1 |
| P57771-1 | ENSG00000135824.13 | ENST00000515211.2 | ENSP00000511884.1 |
| P57771-2 | ENSG00000135824.13 | ENST00000258302.8 | ENSP00000258302.4 |
| UniProt-id | NM ID | NP ID |
| P57771-1 | NM_001102450.2 | NP_001095920.1 |
| P57771-2 | NM_033345.3 | NP_203131.1 |
| P57771-2 | XM_011510089.2 | XP_011508391.1 |
| P57771-2 | XM_017002631.1 | XP_016858120.1 |
| Amino acid sequences of our canonical and alternatively spliced RGS8 |
| accession_id | Protein sequence |
| P57771-1 | MAALLMPRRNKGMRTRLGCLSHKSDSCSDFTAILPDKPNRALKRLSTEEATRWADSFDVLLSHKYGVAAFRAFLKTEFSEENLEFWLACE EFKKTRSTAKLVSKAHRIFEEFVDVQAPREVNIDFQTREATRKNLQEPSLTCFDQAQGKVHSLMEKDSYPRFLRSKMYLDLLSQSQRRLS |
| P57771-2 | MWNTLTRSLSDHPVGKDPQAMRTGQRQNKGMRTRLGCLSHKSDSCSDFTAILPDKPNRALKRLSTEEATRWADSFDVLLSHKYGVAAFRA FLKTEFSEENLEFWLACEEFKKTRSTAKLVSKAHRIFEEFVDVQAPREVNIDFQTREATRKNLQEPSLTCFDQAQGKVHSLMEKDSYPRF |
Protein Functional Features |
| Main function of this protein. (from UniProt) |
| RGS8 (go to UniProt):P57771 |
| Retention analysis result of protein across 39 protein features of UniProt such as six molecule processing features, 13 region features, four site features, six amino acid modification features, two natural variation features, five experimental info features, and 3 secondary structure features. Here, because of limited space for viewing, we only show the protein feature retention information belong to the 13 regional features. All retention annotation result can be downloaded at * Minus value of BPloci means that the break pointn is located before the CDS. |
| - Retained protein feature among the 13 regional features. |
| Accession_id | Subsection | Start | End | Funcitonal feature | Splicing information |
Gene Isoform Structures and Expression Levels for RGS8 |
| Gene structures of our canonical and alternative spliced genes of RGS8 * Click on the image to open the UCSC genome browser with custom track showing this image in a new window. |
| Expression levels of gene isoforms across GTEx. |
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| Expression levels of gene isoforms across TCGA. |
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Protein Structures |
| PDB and CIF files of the predicted protein structures * Here we show the 3D structure of the proteins using Mol*. AlphaFold produces a per-residue confidence score (pLDDT) between 0 and 100. Model confidence is shown from the pLDDT values per residue. pLDDT corresponds to the model’s prediction of its score on the local Distance Difference Test. It is a measure of local accuracy (from AlphfaFold website). To color code individual residues, we transformed individual PDB files into CIF format. |
| 3D view using mol* of P57771-1 |
| 3D view using mol* of P57771-2 |
pLDDT Score Distribution |
| pLDDT score distribution of the predicted protein structures from AlphaFold2 * AlphaFold produces a per-residue confidence score (pLDDT) between 0 and 100. |
| pLDDT distribution across the protein length of P57771-1 |
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| pLDDT distribution across the protein length of P57771-2 |
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Ramachandran Plot of Protein Structures |
| Ramachandran plot of the torsional angles - phi (φ)and psi (ψ) - of the residues (amino acids) contained in this protein peptide. |
| Ramachandran plot of P57771-1 |
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| Ramachandran plot of P57771-2 |
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Potential Active Site Information |
| The potential binding sites of these proteins were identified using SiteMap, a module of the Schrodinger suite. |
| UniProt-id | Site score | Size | D score | Volume | Exposure | Enclosure | Contact | Phobic | Philic | Balance | Don/Acc | Residues |
| P57771-1 | 1.052 | 110 | 1.107 | 248.332 | 0.52 | 0.699 | 0.972 | 1.333 | 0.776 | 1.718 | 0.669 | 27,28,29,30,31,33,34,42,43,45,50,53,65,68,69,165,1 66,167,170,171,174,175,178 |
| P57771-2 | 0.991 | 127 | 1.033 | 377.986 | 0.604 | 0.645 | 0.868 | 0.572 | 0.902 | 0.634 | 0.903 | 46,47,48,49,52,54,55,56,57,58,59,60,61,62,63,64,65 ,66,68,71,87,183,184,185,188,189,190,192,193,196,1 97 |
Protein Structure and Feature Comparision |
| Protein Structure Comparision Using Template Modeling Scores (TM-score). |
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| Protein Structure Comparision Visualization with mol*. between Canonical predicted structure (AF2)(orange) vs Canonical validated structure (PDB)(green) |
| 3D view using mol* of P57771-1_P57771-1_5do9_B.pdb |
| Protein Structure Comparision Visualization with mol*. between Canonical validated structure (PDB)(orange) vs Alternative predicted structure (AF2)(green) |
| 3D view using mol* of P57771-1_5do9_B_P57771-2.pdb |
| Protein Structure Comparision Visualization with mol*. between Canonical predicted structure (AF2)(orange) vs Alternative predicted structure (AF2)(green) |
| 3D view using mol* of P57771-1_P57771-2.pdb |
| Protein Feature Comparison of the protein sequendary structures among the protiens. |
| ./stats/secondary_structure/figure/P57771-1_vs_P57771-2.png |
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| Protein Feature Comparison of the relative accessible surface area (ASA) among the protiens. |
| ./stats/relative_asa/P57771-1_vs_P57771-2.png |
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Protein-Protein Interaction |
| Interactors from UniProt. |
| Accession_id | Subsection | Start | End | Funcitonal feature | Splicing information |
| Interactors from STRING. |
| Gene name | Interactors |
Related Drugs to RGS8 |
| Drugs targeting this gene/protein. (DrugBank) |
| UniProt accession | Gene name | DrugBank ID | Drug name | Drug group | Actions |
Related Diseases to RGS8 |
| Previous studies relating to the alternative splicing of RGS8 and disease information from the MeSH term (PubMed) |
| Gene | PMID | Title | Abstract | MeSH ID | MeSH term |
| RGS8 | 12110731 | Alternative splicing of RGS8 gene determines inhibitory function of receptor type-specific Gq signaling. | The regulators of G protein signaling (RGS) proteins modulate heterotrimeric G protein signaling. RGS8 is a brain-specific RGS protein of 180 aa. Here we identified a short isoform of RGS8, RGS8S, that arises by alternative splicing. RGS8S cDNA encodes a N terminus of 7 aa instead of amino acids 1-9 of RGS8 and 10-180 of RGS8. The subcellular distribution of RGS8 and RGS8S did not differ significantly in transfected cells. RGS8S accelerated, not as efficiently as RGS8, the turning on and off of Gi/o-mediated modulation of G protein-gated inwardly rectifying K(+) channels in Xenopus oocytes. We next examined the effects of RGS8 and RGS8S on Gq-mediated signaling. RGS8 decreased the amplitude of the response upon activation of m1 muscarinic or substance P receptors, but did not remarkably inhibit signaling from m3 muscarinic receptors. In contrast, RGS8S showed much less inhibition of the response of either of these Gq-coupled receptors. By quantitative analysis of the inhibitory effect and the protein expression level, we confirmed that the difference of inhibitory effect is caused by both the qualitative difference between RGS8 and RGS8S and the quantitative difference of the protein expression level. We also confirmed that the receptor-type specificity of inhibition is not caused by the difference of the expression level of the receptors. In summary, we showed that 9 aa in the N terminus of RGS8 contribute to the function to inhibit Gq-coupled signaling in a receptor type-specific manner and that the regulatory function of RGS8S is especially diminished on Gq-coupled responses. | D007890 | Leiomyosarcoma |
Clinically important variants in RGS8 |
| (ClinVar, 04/20/2024) |
| accession_id | uniprot_id | gene_name | Type | Variant | Clinical_significance |
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