Protein:REST |
Protein Summary |
 Gene summary |
| Gene name: REST | ASpdb.0 ID: 5978 | Gene | Gene symbol | REST | Gene ID | 5978 |
| Gene name | RE1 silencing transcription factor |
| Synonyms | DFNA27|GINGF5|HGF5|NRSF|WT6|XBR |
| Cytomap | 4q12 |
| Type of gene | protein-coding |
| Description | RE1-silencing transcription factorneural-restrictive silencer factorneuron restrictive silencer factorrepressor binding to the X2 box |
| Modification date | 20240403 |
| UniProtAcc | Q13127 |
| Gene ontology of this gene with evidence of Inferred from Direct Assay (IDA) from Entrez |
| Partner | Gene | GO ID | GO term | PubMed ID |
| Gene | REST | GO:0000122 | negative regulation of transcription by RNA polymerase II | 8568247|21284946 |
| Gene | REST | GO:0000976 | transcription cis-regulatory region binding | 17555596 |
| Gene | REST | GO:0000978 | RNA polymerase II cis-regulatory region sequence-specific DNA binding | 8568247|17984088 |
| Gene | REST | GO:0001227 | DNA-binding transcription repressor activity, RNA polymerase II-specific | 10449787|10734093|21284946 |
| Gene | REST | GO:0001666 | response to hypoxia | 27531581 |
| Gene | REST | GO:0003700 | DNA-binding transcription factor activity | 19342457 |
| Gene | REST | GO:0005634 | nucleus | 7697725|10734093|16417580|16442230|17984088|19342457|21258371|21284946|24670762|27531581|30684677 |
| Gene | REST | GO:0005654 | nucleoplasm | - |
| Gene | REST | GO:0005737 | cytoplasm | 24670762|27531581|30684677 |
| Gene | REST | GO:0005829 | cytosol | - |
| Gene | REST | GO:0017053 | transcription repressor complex | 10734093 |
| Gene | REST | GO:0043922 | negative regulation by host of viral transcription | 17555596 |
| Gene | REST | GO:0045665 | negative regulation of neuron differentiation | 21258371 |
| Gene | REST | GO:0045892 | negative regulation of DNA-templated transcription | 7697725|10449787|10734093|11741002|11779185|17984088|19342457 |
| Gene | REST | GO:0045893 | positive regulation of DNA-templated transcription | 17984088 |
| Gene | REST | GO:0071385 | cellular response to glucocorticoid stimulus | 17984088 |
| Gene | REST | GO:1902459 | positive regulation of stem cell population maintenance | 21258371 |
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 |
| Q13127-1 | Q13127-1_6du3_C.pdb | 6DU3 | X-ray | 2.58 | C | 859 | 865 |
| 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 |
| Q13127 | REST | Q13127-1 | Q13127-2 | 1097 | 313 | 301 | 313 | Substitution | ERPYKCELCPYSS | KRSFLVHKFSSLF | 301 | 313 |
| Q13127 | REST | Q13127-1 | Q13127-2 | 1097 | 313 | 314 | 1097 | Deletion | none | none | 313 | 313 |
| Q13127 | REST | Q13127-1 | Q13127-3 | 1097 | 329 | 329 | 329 | Substitution | E | W | 329 | 329 |
| Q13127 | REST | Q13127-1 | Q13127-3 | 1097 | 329 | 330 | 1097 | Deletion | none | none | 329 | 329 |
| Q13127 | REST | Q13127-1 | Q13127-4 | 1097 | 1074 | 304 | 326 | Deletion | none | none | 303 | 303 |
| Multiple sequence alignment of our canonical and alternatively spliced REST |
| Matched gene isoform IDs with Ensembl and RefSeq of our canonical and alternative spliced genes of REST |
| UniProt-id | ENSG | ENST | ENSP |
| Q13127-1 | ENSG00000084093.19 | ENST00000309042.12 | ENSP00000311816.7 |
| Q13127-1 | ENSG00000084093.19 | ENST00000675105.1 | ENSP00000502313.1 |
| UniProt-id | NM ID | NP ID |
| Q13127-1 | NM_001193508.1 | NP_001180437.1 |
| Q13127-1 | NM_005612.4 | NP_005603.3 |
| Amino acid sequences of our canonical and alternatively spliced REST |
| accession_id | Protein sequence |
| Q13127-1 | MATQVMGQSSGGGGLFTSSGNIGMALPNDMYDLHDLSKAELAAPQLIMLANVALTGEVNGSCCDYLVGEERQMAELMPVGDNNFSDSEEG EGLEESADIKGEPHGLENMELRSLELSVVEPQPVFEASGAPDIYSSNKDLPPETPGAEDKGKSSKTKPFRCKPCQYEAESEEQFVHHIRV HSAKKFFVEESAEKQAKARESGSSTAEEGDFSKGPIRCDRCGYNTNRYDHYTAHLKHHTRAGDNERVYKCIICTYTTVSEYHWRKHLRNH FPRKVYTCGKCNYFSDRKNNYVQHVRTHTGERPYKCELCPYSSSQKTHLTRHMRTHSGEKPFKCDQCSYVASNQHEVTRHARQVHNGPKP LNCPHCDYKTADRSNFKKHVELHVNPRQFNCPVCDYAASKKCNLQYHFKSKHPTCPNKTMDVSKVKLKKTKKREADLPDNITNEKTEIEQ TKIKGDVAGKKNEKSVKAEKRDVSKEKKPSNNVSVIQVTTRTRKSVTEVKEMDVHTGSNSEKFSKTKKSKRKLEVDSHSLHGPVNDEESS TKKKKKVESKSKNNSQEVPKGDSKVEENKKQNTCMKKSTKKKTLKNKSSKKSSKPPQKEPVEKGSAQMDPPQMGPAPTEAVQKGPVQVEP PPPMEHAQMEGAQIRPAPDEPVQMEVVQEGPAQKELLPPVEPAQMVGAQIVLAHMELPPPMETAQTEVAQMGPAPMEPAQMEVAQVESAP MQVVQKEPVQMELSPPMEVVQKEPVQIELSPPMEVVQKEPVKIELSPPIEVVQKEPVQMELSPPMGVVQKEPAQREPPPPREPPLHMEPI SKKPPLRKDKKEKSNMQSERARKEQVLIEVGLVPVKDSWLLKESVSTEDLSPPSPPLPKENLREEASGDQKLLNTGEGNKEAPLQKVGAE EADESLPGLAANINESTHISSSGQNLNTPEGETLNGKHQTDSIVCEMKMDTDQNTRENLTGINSTVEEPVSPMLPPSAVEEREAVSKTAL ASPPATMAANESQEIDEDEGIHSHEGSDLSDNMSEGSDDSGLHGARPVPQESSRKNAKEALAVKAAKGDFVCIFCDRSFRKGKDYSKHLN |
| Q13127-2 | MATQVMGQSSGGGGLFTSSGNIGMALPNDMYDLHDLSKAELAAPQLIMLANVALTGEVNGSCCDYLVGEERQMAELMPVGDNNFSDSEEG EGLEESADIKGEPHGLENMELRSLELSVVEPQPVFEASGAPDIYSSNKDLPPETPGAEDKGKSSKTKPFRCKPCQYEAESEEQFVHHIRV HSAKKFFVEESAEKQAKARESGSSTAEEGDFSKGPIRCDRCGYNTNRYDHYTAHLKHHTRAGDNERVYKCIICTYTTVSEYHWRKHLRNH |
| Q13127-3 | MATQVMGQSSGGGGLFTSSGNIGMALPNDMYDLHDLSKAELAAPQLIMLANVALTGEVNGSCCDYLVGEERQMAELMPVGDNNFSDSEEG EGLEESADIKGEPHGLENMELRSLELSVVEPQPVFEASGAPDIYSSNKDLPPETPGAEDKGKSSKTKPFRCKPCQYEAESEEQFVHHIRV HSAKKFFVEESAEKQAKARESGSSTAEEGDFSKGPIRCDRCGYNTNRYDHYTAHLKHHTRAGDNERVYKCIICTYTTVSEYHWRKHLRNH |
| Q13127-4 | MATQVMGQSSGGGGLFTSSGNIGMALPNDMYDLHDLSKAELAAPQLIMLANVALTGEVNGSCCDYLVGEERQMAELMPVGDNNFSDSEEG EGLEESADIKGEPHGLENMELRSLELSVVEPQPVFEASGAPDIYSSNKDLPPETPGAEDKGKSSKTKPFRCKPCQYEAESEEQFVHHIRV HSAKKFFVEESAEKQAKARESGSSTAEEGDFSKGPIRCDRCGYNTNRYDHYTAHLKHHTRAGDNERVYKCIICTYTTVSEYHWRKHLRNH FPRKVYTCGKCNYFSDRKNNYVQHVRTHTGERPSGEKPFKCDQCSYVASNQHEVTRHARQVHNGPKPLNCPHCDYKTADRSNFKKHVELH VNPRQFNCPVCDYAASKKCNLQYHFKSKHPTCPNKTMDVSKVKLKKTKKREADLPDNITNEKTEIEQTKIKGDVAGKKNEKSVKAEKRDV SKEKKPSNNVSVIQVTTRTRKSVTEVKEMDVHTGSNSEKFSKTKKSKRKLEVDSHSLHGPVNDEESSTKKKKKVESKSKNNSQEVPKGDS KVEENKKQNTCMKKSTKKKTLKNKSSKKSSKPPQKEPVEKGSAQMDPPQMGPAPTEAVQKGPVQVEPPPPMEHAQMEGAQIRPAPDEPVQ MEVVQEGPAQKELLPPVEPAQMVGAQIVLAHMELPPPMETAQTEVAQMGPAPMEPAQMEVAQVESAPMQVVQKEPVQMELSPPMEVVQKE PVQIELSPPMEVVQKEPVKIELSPPIEVVQKEPVQMELSPPMGVVQKEPAQREPPPPREPPLHMEPISKKPPLRKDKKEKSNMQSERARK EQVLIEVGLVPVKDSWLLKESVSTEDLSPPSPPLPKENLREEASGDQKLLNTGEGNKEAPLQKVGAEEADESLPGLAANINESTHISSSG QNLNTPEGETLNGKHQTDSIVCEMKMDTDQNTRENLTGINSTVEEPVSPMLPPSAVEEREAVSKTALASPPATMAANESQEIDEDEGIHS |
Protein Functional Features |
| Main function of this protein. (from UniProt) |
| REST (go to UniProt):Q13127 |
| 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 |
| Q13127 | Zinc finger | 304 | 326 | Note=C2H2-type 5;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00042 | Type=Substitution;Start=301;End=313 |
| Q13127 | Zinc finger | 304 | 326 | Note=C2H2-type 5;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00042 | Type=Deletion;Start=314;End=1097 |
| Q13127 | Zinc finger | 304 | 326 | Note=C2H2-type 5;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00042 | Type=Deletion;Start=304;End=326 |
| Q13127 | Zinc finger | 332 | 355 | Note=C2H2-type 6;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00042 | Type=Deletion;Start=314;End=1097 |
| Q13127 | Zinc finger | 332 | 355 | Note=C2H2-type 6;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00042 | Type=Deletion;Start=330;End=1097 |
| Q13127 | Zinc finger | 361 | 383 | Note=C2H2-type 7;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00042 | Type=Deletion;Start=314;End=1097 |
| Q13127 | Zinc finger | 361 | 383 | Note=C2H2-type 7;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00042 | Type=Deletion;Start=330;End=1097 |
| Q13127 | Zinc finger | 389 | 412 | Note=C2H2-type 8;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00042 | Type=Deletion;Start=314;End=1097 |
| Q13127 | Zinc finger | 389 | 412 | Note=C2H2-type 8;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00042 | Type=Deletion;Start=330;End=1097 |
| Q13127 | Zinc finger | 1060 | 1082 | Note=C2H2-type 9;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00042 | Type=Deletion;Start=314;End=1097 |
| Q13127 | Zinc finger | 1060 | 1082 | Note=C2H2-type 9;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00042 | Type=Deletion;Start=330;End=1097 |
| Q13127 | Region | 145 | 418 | Note=Interaction with ZFP90;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:21284946;Dbxref=PMID:21284946 | Type=Substitution;Start=301;End=313 |
| Q13127 | Region | 145 | 418 | Note=Interaction with ZFP90;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:21284946;Dbxref=PMID:21284946 | Type=Deletion;Start=314;End=1097 |
| Q13127 | Region | 145 | 418 | Note=Interaction with ZFP90;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:21284946;Dbxref=PMID:21284946 | Type=Substitution;Start=329;End=329 |
| Q13127 | Region | 145 | 418 | Note=Interaction with ZFP90;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:21284946;Dbxref=PMID:21284946 | Type=Deletion;Start=330;End=1097 |
| Q13127 | Region | 145 | 418 | Note=Interaction with ZFP90;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:21284946;Dbxref=PMID:21284946 | Type=Deletion;Start=304;End=326 |
| Q13127 | Region | 452 | 642 | Note=Disordered;Ontology_term=ECO:0000256;evidence=ECO:0000256|SAM:MobiDB-lite | Type=Deletion;Start=314;End=1097 |
| Q13127 | Region | 452 | 642 | Note=Disordered;Ontology_term=ECO:0000256;evidence=ECO:0000256|SAM:MobiDB-lite | Type=Deletion;Start=330;End=1097 |
| Q13127 | Region | 774 | 837 | Note=Disordered;Ontology_term=ECO:0000256;evidence=ECO:0000256|SAM:MobiDB-lite | Type=Deletion;Start=314;End=1097 |
| Q13127 | Region | 774 | 837 | Note=Disordered;Ontology_term=ECO:0000256;evidence=ECO:0000256|SAM:MobiDB-lite | Type=Deletion;Start=330;End=1097 |
| Q13127 | Region | 853 | 938 | Note=Disordered;Ontology_term=ECO:0000256;evidence=ECO:0000256|SAM:MobiDB-lite | Type=Deletion;Start=314;End=1097 |
| Q13127 | Region | 853 | 938 | Note=Disordered;Ontology_term=ECO:0000256;evidence=ECO:0000256|SAM:MobiDB-lite | Type=Deletion;Start=330;End=1097 |
| Q13127 | Region | 961 | 1049 | Note=Disordered;Ontology_term=ECO:0000256;evidence=ECO:0000256|SAM:MobiDB-lite | Type=Deletion;Start=314;End=1097 |
| Q13127 | Region | 961 | 1049 | Note=Disordered;Ontology_term=ECO:0000256;evidence=ECO:0000256|SAM:MobiDB-lite | Type=Deletion;Start=330;End=1097 |
| Q13127 | Region | 1009 | 1087 | Note=Interaction with RCOR1;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:10449787;Dbxref=PMID:10449787 | Type=Deletion;Start=314;End=1097 |
| Q13127 | Region | 1009 | 1087 | Note=Interaction with RCOR1;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:10449787;Dbxref=PMID:10449787 | Type=Deletion;Start=330;End=1097 |
| Q13127 | Compositional bias | 452 | 478 | Note=Basic and acidic residues;Ontology_term=ECO:0000256;evidence=ECO:0000256|SAM:MobiDB-lite | Type=Deletion;Start=314;End=1097 |
| Q13127 | Compositional bias | 452 | 478 | Note=Basic and acidic residues;Ontology_term=ECO:0000256;evidence=ECO:0000256|SAM:MobiDB-lite | Type=Deletion;Start=330;End=1097 |
| Q13127 | Compositional bias | 479 | 493 | Note=Polar residues;Ontology_term=ECO:0000256;evidence=ECO:0000256|SAM:MobiDB-lite | Type=Deletion;Start=314;End=1097 |
| Q13127 | Compositional bias | 479 | 493 | Note=Polar residues;Ontology_term=ECO:0000256;evidence=ECO:0000256|SAM:MobiDB-lite | Type=Deletion;Start=330;End=1097 |
| Q13127 | Compositional bias | 494 | 574 | Note=Basic and acidic residues;Ontology_term=ECO:0000256;evidence=ECO:0000256|SAM:MobiDB-lite | Type=Deletion;Start=314;End=1097 |
| Q13127 | Compositional bias | 494 | 574 | Note=Basic and acidic residues;Ontology_term=ECO:0000256;evidence=ECO:0000256|SAM:MobiDB-lite | Type=Deletion;Start=330;End=1097 |
| Q13127 | Compositional bias | 575 | 591 | Note=Basic residues;Ontology_term=ECO:0000256;evidence=ECO:0000256|SAM:MobiDB-lite | Type=Deletion;Start=314;End=1097 |
| Q13127 | Compositional bias | 575 | 591 | Note=Basic residues;Ontology_term=ECO:0000256;evidence=ECO:0000256|SAM:MobiDB-lite | Type=Deletion;Start=330;End=1097 |
| Q13127 | Compositional bias | 806 | 836 | Note=Basic and acidic residues;Ontology_term=ECO:0000256;evidence=ECO:0000256|SAM:MobiDB-lite | Type=Deletion;Start=314;End=1097 |
| Q13127 | Compositional bias | 806 | 836 | Note=Basic and acidic residues;Ontology_term=ECO:0000256;evidence=ECO:0000256|SAM:MobiDB-lite | Type=Deletion;Start=330;End=1097 |
| Q13127 | Compositional bias | 910 | 938 | Note=Polar residues;Ontology_term=ECO:0000256;evidence=ECO:0000256|SAM:MobiDB-lite | Type=Deletion;Start=314;End=1097 |
| Q13127 | Compositional bias | 910 | 938 | Note=Polar residues;Ontology_term=ECO:0000256;evidence=ECO:0000256|SAM:MobiDB-lite | Type=Deletion;Start=330;End=1097 |
| Q13127 | Compositional bias | 1005 | 1021 | Note=Basic and acidic residues;Ontology_term=ECO:0000256;evidence=ECO:0000256|SAM:MobiDB-lite | Type=Deletion;Start=314;End=1097 |
| Q13127 | Compositional bias | 1005 | 1021 | Note=Basic and acidic residues;Ontology_term=ECO:0000256;evidence=ECO:0000256|SAM:MobiDB-lite | Type=Deletion;Start=330;End=1097 |
Gene Isoform Structures and Expression Levels for REST |
| Gene structures of our canonical and alternative spliced genes of REST * 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 Q13127-1 |
| 3D view using mol* of Q13127-2 |
| 3D view using mol* of Q13127-3 |
| 3D view using mol* of Q13127-4 |
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 Q13127-1 |
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| pLDDT distribution across the protein length of Q13127-2 |
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| pLDDT distribution across the protein length of Q13127-3 |
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| pLDDT distribution across the protein length of Q13127-4 |
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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 Q13127-1 |
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| Ramachandran plot of Q13127-2 |
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| Ramachandran plot of Q13127-3 |
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| Ramachandran plot of Q13127-4 |
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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 |
| Q13127-1 | 1.032 | 129 | 1.106 | 423.262 | 0.663 | 0.639 | 0.837 | 0.924 | 0.667 | 1.385 | 1.803 | 46,49,50,53,54,252,264,267,268,270,271,272,273,274 ,275,284,1085,1086,1088,1089,1090,1092,1093,1096 |
| Q13127-2 | 0.871 | 73 | 0.903 | 181.104 | 0.697 | 0.588 | 0.694 | 0.457 | 0.774 | 0.59 | 1.101 | 223,224,225,226,230,233,234,237,254,255,256,257,25 8,259,262,265,266 |
| Q13127-3 | 0.98 | 96 | 1.015 | 277.487 | 0.595 | 0.654 | 0.856 | 0.822 | 0.917 | 0.897 | 0.681 | 51,55,58,59,60,61,62,63,260,261,264,267,268,271,27 3 |
| Q13127-4 | 0.919 | 79 | 0.935 | 327.222 | 0.711 | 0.663 | 0.718 | 0.22 | 0.917 | 0.24 | 0.548 | 223,224,225,226,230,233,234,237,255,256,257,258,25 9,261,262,265,266,269,287 |
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 Q13127-1_Q13127-1_6du3_C.pdb |
| Protein Structure Comparision Visualization with mol*. between Canonical validated structure (PDB)(orange) vs Alternative predicted structure (AF2)(green) |
| 3D view using mol* of Q13127-1_6du3_C_Q13127-2.pdb |
| 3D view using mol* of Q13127-1_6du3_C_Q13127-3.pdb |
| 3D view using mol* of Q13127-1_6du3_C_Q13127-4.pdb |
| Protein Structure Comparision Visualization with mol*. between Canonical predicted structure (AF2)(orange) vs Alternative predicted structure (AF2)(green) |
| 3D view using mol* of Q13127-1_Q13127-2.pdb |
| 3D view using mol* of Q13127-1_Q13127-3.pdb |
| 3D view using mol* of Q13127-1_Q13127-4.pdb |
| Protein Feature Comparison of the protein sequendary structures among the protiens. |
| ./stats/secondary_structure/figure/Q13127-1_vs_Q13127-2.png |
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| ./stats/secondary_structure/figure/Q13127-1_vs_Q13127-3.png |
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| ./stats/secondary_structure/figure/Q13127-1_vs_Q13127-4.png |
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| Protein Feature Comparison of the relative accessible surface area (ASA) among the protiens. |
| ./stats/relative_asa/Q13127-1_vs_Q13127-2.png |
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| ./stats/relative_asa/Q13127-1_vs_Q13127-3.png |
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| ./stats/relative_asa/Q13127-1_vs_Q13127-4.png |
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Protein-Protein Interaction |
| Interactors from UniProt. |
| Accession_id | Subsection | Start | End | Funcitonal feature | Splicing information |
| Q13127 | Region | 145 | 418 | Note=Interaction with ZFP90;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:21284946;Dbxref=PMID:21284946 | Type=Substitution;Start=301;End=313 |
| Q13127 | Region | 145 | 418 | Note=Interaction with ZFP90;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:21284946;Dbxref=PMID:21284946 | Type=Deletion;Start=314;End=1097 |
| Q13127 | Region | 145 | 418 | Note=Interaction with ZFP90;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:21284946;Dbxref=PMID:21284946 | Type=Substitution;Start=329;End=329 |
| Q13127 | Region | 145 | 418 | Note=Interaction with ZFP90;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:21284946;Dbxref=PMID:21284946 | Type=Deletion;Start=330;End=1097 |
| Q13127 | Region | 145 | 418 | Note=Interaction with ZFP90;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:21284946;Dbxref=PMID:21284946 | Type=Deletion;Start=304;End=326 |
| Q13127 | Region | 1009 | 1087 | Note=Interaction with RCOR1;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:10449787;Dbxref=PMID:10449787 | Type=Deletion;Start=314;End=1097 |
| Q13127 | Region | 1009 | 1087 | Note=Interaction with RCOR1;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:10449787;Dbxref=PMID:10449787 | Type=Deletion;Start=330;End=1097 |
| Interactors from STRING. |
| Gene name | Interactors |
Related Drugs to REST |
| Drugs targeting this gene/protein. (DrugBank) |
| UniProt accession | Gene name | DrugBank ID | Drug name | Drug group | Actions |
Related Diseases to REST |
| Previous studies relating to the alternative splicing of REST and disease information from the MeSH term (PubMed) |
| Gene | PMID | Title | Abstract | MeSH ID | MeSH term |
| REST | 20548947 | The transcription factor REST is lost in aggressive breast cancer. | The function of the tumor suppressor RE1 silencing transcription factor (REST) is lost in colon and small cell lung cancers and is known to induce anchorage-independent growth in human mammary epithelial cells. However, nothing is currently known about the role of this tumor suppressor in breast cancer. Here, we test the hypothesis that loss of REST function plays a role in breast cancer. To assay breast tumors for REST function, we developed a 24-gene signature composed of direct targets of the transcriptional repressor. Using the 24- gene signature, we identified a previously undefined RESTless breast tumor subtype. Using gene set enrichment analysis, we confirmed the aberrant expression of REST target genes in the REST-less tumors, including neuronal gene targets of REST that are normally not expressed outside the nervous system. Examination of REST mRNA identified a truncated splice variant of REST present in the REST-less tumor population, but not other tumors. Histological analysis of 182 outcome-associated breast tumor tissues also identified a subpopulation of tumors that lack full-length, functional REST and over-express the neuroendocrine marker and REST target gene Chromogranin A. Importantly, patients whose tumors were found to be REST-less using either the 24-gene signature or histology had significantly poorer prognosis and were more than twice as likely to undergo disease recurrence within the first 3 years after diagnosis. We show here that REST function is lost in breast cancer, at least in part via an alternative splicing mechanism. Patients with REST-less breast cancer undergo significantly more early disease recurrence than those with fully functional REST, regardless of estrogen receptor or HER2 status. Importantly, REST status may serve as a predictor of poor prognosis, helping to untangle the heterogeneity inherent in disease course and response to treatment. Additionally, the alternative splicing observed in REST-less breast cancer is an attractive therapeutic target. | D001943 | Breast Neoplasms |
| REST | 23614038 | Extensive alternative splicing of the repressor element silencing transcription factor linked to cancer. | The repressor element silencing transcription factor (REST) is a coordinate transcriptional and epigenetic regulator which functions as a tumor suppressor or an oncogene depending on cellular context, and a truncated splice variant REST4 has been linked to various types of cancer. We performed a comprehensive analysis of alternative splicing (AS) of REST by rapid amplification of cDNA ends and PCR amplification of cDNAs from various tissues and cell lines with specific primers. We identified 8 novel alternative exons including an alternate last exon which doubles the REST gene boundary, along with numerous 5'/3' splice sites and ends in the constitutive exons. With the combination of various splicing patterns (e.g. exon skipping and alternative usage of the first and last exons) that are predictive of altered REST activity, at least 45 alternatively spliced variants of coding and non-coding mRNA were expressed in a species- and cell-type/tissue-specific manner with individual differences. By examining the repertoire of REST pre-mRNA splicing in 27 patients with kidney, liver and lung cancer, we found that all patients without exception showed differential expression of various REST splice variants between paired tumor and adjacent normal tissues, with striking cell-type/tissue and individual differences. Moreover, we revealed that exon 3 skipping, which causes no frame shift but loss of a domain essential for nuclear translocation, was affected by pioglitazone, a highly selective activator of the peroxisome proliferator-activated receptor gamma (PPARγ) which contributes to cell differentiation and tumorigenesis besides its metabolic actions. Accordingly, this study demonstrates an extensive AS of REST pre-mRNA which redefines REST gene boundary and structure, along with a general but differential link between REST pre-mRNA splicing and various types of cancer. These findings advance our understanding of the complex, context-dependent regulation of REST gene expression and function, and provide potential biomarkers and therapeutic targets for cancer. | D009369 | Neoplasms |
| REST | 23928058 | The small cell lung cancer-specific isoform of RE1-silencing transcription factor (REST) is regulated by neural-specific Ser/Arg repeat-related protein of 100 kDa (nSR100). | Small cell lung cancer (SCLC) is a highly malignant form of cancer, which originates from primitive neuroendocrine cells in the lung. SCLC cells express several autocrine neurotransmitters/neuropeptides and their respective receptors. Expression of these neuronal markers is frequently regulated by RE1-silencing transcription factor (REST). In SCLC cells, an SCLC-specific isoform of REST (sREST) is highly expressed, whereas REST expression is undetectable, suggesting that the expression of sREST correlates with the pathogenesis of SCLC. Expression of sREST, which is derived through alternative splicing of REST, is abnormally regulated in SCLC cells, but the mechanism is unknown. Most recently, nSR100 (SRRM4) was described as an activator of REST alternative splicing. We now show that nSR100 is highly expressed in SCLC cells correlating with high sREST and low REST expression. Adhesion to the extracellular matrix (ECM) is thought to enhance tumorigenicity and confer resistance to apoptosis. Interestingly, nSR100 expression is enhanced in cells grown with ECM. Overexpression of REST caused repression of sREST and nSR100, the latter containing RE1 element controlled by REST. Culturing the SCLC cell line NCI-N417 cells with ECM also upregulated RE1-containing gene, the voltage-gated calcium channel subunit. Inhibition of the PI3K/Akt/mTOR pathway by LY294002 induced nSR100 expression, whereas the specific MEK/ERK inhibitor U0126 inhibited nSR100 expression. Repressing nSR100 by siRNA effectively repressed sREST, and conversely increased REST in NCI-N417 cells. Taken together, this report clarifies the ECM-dependent signaling pathway that impacts nSR100 expression and its regulation of alternative splicing in SCLC. | D055752 | Small Cell Lung Carcinoma |
| REST | 26003726 | Expression of REST4 in human gliomas in vivo and influence of pioglitazone on REST in vitro. | The repressor element-1 (RE1) silencing transcription factor/neuron-restrictive silencer factor (REST/NRSF) has an irreplaceable role during the differentiation of neurons. REST has multiple splice variants which link to various types of cancer. Previous work had highlighted the role of REST in glioma, where the expression of REST is enhanced. But whether alternative splicing of REST is expressed in glioma has not been described. Here, we show that a specific isoform REST4 is expressed in glioma specimens, and will influence the mRNA level of REST in vivo. Peroxisome proliferator-activated receptor-γ (PPARγ) agonists have a role of antineoplastic in various tumor cells, which including glioma cells. Moreover, study indicated that PPARγ agonist pioglitazone can promote alternative splicing of REST pre-mRNA. In this study, we selected pioglitazone as a tool drug to explore whether the role of pioglitazone in anti-glioma is mediated by regulating REST expression or promoting alternative splicing of REST in glioma cells. Results show that pioglitazone can inhibit proliferation and induce apoptosis of glioma cell in vitro, which may be mediated by down-regulating REST mRNA level but not by inducing alternative splicing of REST pre-mRNA. Our study firstly reports the expression of REST4 in glioma tissue samples. And we recommend that pioglitazone, which can reduce the expression level of REST, represents a promising drug for therapy of glioma. | D001932 | Brain Neoplasms |
| REST | 26003726 | Expression of REST4 in human gliomas in vivo and influence of pioglitazone on REST in vitro. | The repressor element-1 (RE1) silencing transcription factor/neuron-restrictive silencer factor (REST/NRSF) has an irreplaceable role during the differentiation of neurons. REST has multiple splice variants which link to various types of cancer. Previous work had highlighted the role of REST in glioma, where the expression of REST is enhanced. But whether alternative splicing of REST is expressed in glioma has not been described. Here, we show that a specific isoform REST4 is expressed in glioma specimens, and will influence the mRNA level of REST in vivo. Peroxisome proliferator-activated receptor-γ (PPARγ) agonists have a role of antineoplastic in various tumor cells, which including glioma cells. Moreover, study indicated that PPARγ agonist pioglitazone can promote alternative splicing of REST pre-mRNA. In this study, we selected pioglitazone as a tool drug to explore whether the role of pioglitazone in anti-glioma is mediated by regulating REST expression or promoting alternative splicing of REST in glioma cells. Results show that pioglitazone can inhibit proliferation and induce apoptosis of glioma cell in vitro, which may be mediated by down-regulating REST mRNA level but not by inducing alternative splicing of REST pre-mRNA. Our study firstly reports the expression of REST4 in glioma tissue samples. And we recommend that pioglitazone, which can reduce the expression level of REST, represents a promising drug for therapy of glioma. | D005910 | Glioma |
Clinically important variants in REST |
| (ClinVar, 04/20/2024) |
| accession_id | uniprot_id | gene_name | Type | Variant | Clinical_significance |
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