Protein:RNASEL |
Protein Summary |
 Gene summary |
| Gene name: RNASEL | ASpdb.0 ID: 6041 | Gene | Gene symbol | RNASEL | Gene ID | 6041 |
| Gene name | ribonuclease L |
| Synonyms | PRCA1|RNS4 |
| Cytomap | 1q25.3 |
| Type of gene | protein-coding |
| Description | 2-5A-dependent ribonuclease2',5'-oligoisoadenylate synthetase-dependent2-5A-dependent RNaseRNase Linterferon-induced 2-5A-dependent RNaseribonuclease 4 |
| Modification date | 20240403 |
| UniProtAcc | Q05823 |
| Gene ontology of this gene with evidence of Inferred from Direct Assay (IDA) from Entrez |
| Partner | Gene | GO ID | GO term | PubMed ID |
| Gene | RNASEL | GO:0003723 | RNA binding | 7514601 |
| Gene | RNASEL | GO:0004540 | RNA nuclease activity | 23196181 |
| Gene | RNASEL | GO:0045071 | negative regulation of viral genome replication | 19923450|23196181 |
| Gene | RNASEL | GO:0045944 | positive regulation of transcription by RNA polymerase II | 19245366 |
| Gene | RNASEL | GO:0051607 | defense response to virus | 19923450|23196181 |
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 |
| Q05823-1 | Q05823-1_4oau_C.pdb | 4OAU | X-ray | 2.6 | C | 25 | 719 |
| 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 |
| Q05823 | RNASEL | Q05823-1 | Q05823-2 | 741 | 652 | 636 | 652 | Substitution | INECVMKKMNKFYEKRG | MSKLRHRQIIFPTTQNQ | 636 | 652 |
| Q05823 | RNASEL | Q05823-1 | Q05823-2 | 741 | 652 | 653 | 741 | Deletion | none | none | 652 | 652 |
| Multiple sequence alignment of our canonical and alternatively spliced RNASEL |
| Matched gene isoform IDs with Ensembl and RefSeq of our canonical and alternative spliced genes of RNASEL |
| UniProt-id | ENSG | ENST | ENSP |
| Q05823-1 | ENSG00000135828.11 | ENST00000367559.7 | ENSP00000356530.3 |
| Q05823-2 | ENSG00000135828.11 | ENST00000539397.1 | ENSP00000440844.1 |
| UniProt-id | NM ID | NP ID |
| Q05823-1 | NM_021133.3 | NP_066956.1 |
| Amino acid sequences of our canonical and alternatively spliced RNASEL |
| accession_id | Protein sequence |
| Q05823-1 | MESRDHNNPQEGPTSSSGRRAAVEDNHLLIKAVQNEDVDLVQQLLEGGANVNFQEEEGGWTPLHNAVQMSREDIVELLLRHGADPVLRKK NGATPFILAAIAGSVKLLKLFLSKGADVNECDFYGFTAFMEAAVYGKVKALKFLYKRGANVNLRRKTKEDQERLRKGGATALMDAAEKGH VEVLKILLDEMGADVNACDNMGRNALIHALLSSDDSDVEAITHLLLDHGADVNVRGERGKTPLILAVEKKHLGLVQRLLEQEHIEINDTD SDGKTALLLAVELKLKKIAELLCKRGASTDCGDLVMTARRNYDHSLVKVLLSHGAKEDFHPPAEDWKPQSSHWGAALKDLHRIYRPMIGK LKFFIDEKYKIADTSEGGIYLGFYEKQEVAVKTFCEGSPRAQREVSCLQSSRENSHLVTFYGSESHRGHLFVCVTLCEQTLEACLDVHRG EDVENEEDEFARNVLSSIFKAVQELHLSCGYTHQDLQPQNILIDSKKAAHLADFDKSIKWAGDPQEVKRDLEDLGRLVLYVVKKGSISFE DLKAQSNEEVVQLSPDEETKDLIHRLFHPGEHVRDCLSDLLGHPFFWTWESRYRTLRNVGNESDIKTRKSESEILRLLQPGPSEHSKSFD KWTTKINECVMKKMNKFYEKRGNFYQNTVGDLLKFIRNLGEHIDEEKHKKMKLKIGDPSLYFQKTFPDLVIYVYTKLQNTEYRKHFPQTH |
| Q05823-2 | MESRDHNNPQEGPTSSSGRRAAVEDNHLLIKAVQNEDVDLVQQLLEGGANVNFQEEEGGWTPLHNAVQMSREDIVELLLRHGADPVLRKK NGATPFILAAIAGSVKLLKLFLSKGADVNECDFYGFTAFMEAAVYGKVKALKFLYKRGANVNLRRKTKEDQERLRKGGATALMDAAEKGH VEVLKILLDEMGADVNACDNMGRNALIHALLSSDDSDVEAITHLLLDHGADVNVRGERGKTPLILAVEKKHLGLVQRLLEQEHIEINDTD SDGKTALLLAVELKLKKIAELLCKRGASTDCGDLVMTARRNYDHSLVKVLLSHGAKEDFHPPAEDWKPQSSHWGAALKDLHRIYRPMIGK LKFFIDEKYKIADTSEGGIYLGFYEKQEVAVKTFCEGSPRAQREVSCLQSSRENSHLVTFYGSESHRGHLFVCVTLCEQTLEACLDVHRG EDVENEEDEFARNVLSSIFKAVQELHLSCGYTHQDLQPQNILIDSKKAAHLADFDKSIKWAGDPQEVKRDLEDLGRLVLYVVKKGSISFE DLKAQSNEEVVQLSPDEETKDLIHRLFHPGEHVRDCLSDLLGHPFFWTWESRYRTLRNVGNESDIKTRKSESEILRLLQPGPSEHSKSFD |
Protein Functional Features |
| Main function of this protein. (from UniProt) |
| RNASEL (go to UniProt):Q05823 |
| 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 |
| Q05823 | Domain | 589 | 723 | Note=KEN;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00725 | Type=Substitution;Start=636;End=652 |
| Q05823 | Domain | 589 | 723 | Note=KEN;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00725 | Type=Deletion;Start=653;End=741 |
| Q05823 | Region | 715 | 741 | Note=Disordered;Ontology_term=ECO:0000256;evidence=ECO:0000256|SAM:MobiDB-lite | Type=Deletion;Start=653;End=741 |
Gene Isoform Structures and Expression Levels for RNASEL |
| Gene structures of our canonical and alternative spliced genes of RNASEL * 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 Q05823-1 |
| 3D view using mol* of Q05823-2 |
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 Q05823-1 |
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| pLDDT distribution across the protein length of Q05823-2 |
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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 Q05823-1 |
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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 |
| Q05823-1 | 1.083 | 114 | 1.127 | 277.487 | 0.519 | 0.76 | 0.949 | 1.61 | 0.824 | 1.953 | 0.801 | 342,343,371,372,374,375,376,379,390,392,393,400,40 4,418,432,434,436,437,439,440,443,485,487,489,490, 492,502,503,504,505,506 |
| Q05823-2 | 1.094 | 115 | 1.15 | 266.511 | 0.504 | 0.753 | 0.988 | 1.714 | 0.743 | 2.308 | 0.61 | 343,371,372,374,375,379,390,392,400,404,408,418,43 2,434,435,436,437,439,440,443,485,487,489,490,492, 502,503,504,505,506 |
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 Q05823-1_Q05823-1_4oau_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 Q05823-1_4oau_C_Q05823-2.pdb |
| Protein Structure Comparision Visualization with mol*. between Canonical predicted structure (AF2)(orange) vs Alternative predicted structure (AF2)(green) |
| 3D view using mol* of Q05823-1_Q05823-2.pdb |
| Protein Feature Comparison of the protein sequendary structures among the protiens. |
| ./stats/secondary_structure/figure/Q05823-1_vs_Q05823-2.png |
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| Protein Feature Comparison of the relative accessible surface area (ASA) among the protiens. |
| ./stats/relative_asa/Q05823-1_vs_Q05823-2.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 RNASEL |
| Drugs targeting this gene/protein. (DrugBank) |
| UniProt accession | Gene name | DrugBank ID | Drug name | Drug group | Actions |
Related Diseases to RNASEL |
| Previous studies relating to the alternative splicing of RNASEL and disease information from the MeSH term (PubMed) |
| Gene | PMID | Title | Abstract | MeSH ID | MeSH term |
| RNASEL | 12034027 | Structural and functional features of the 37-kDa 2-5A-dependent RNase L in chronic fatigue syndrome. | A 2',5'-oligoadenylate (2-5A)-dependent 37-kDa form of RNase L has been reported in extracts of peripheral blood mononuclear cells (PBMC) from individuals with chronic fatigue syndrome (CFS). In the current study, analytic gel permeation FPLC, azido photoaffinity labeling, two-dimensional (2-D) gel electrophoresis, and matrix-assisted laser desorption/ionization mass spectrometry (MALDI-MS) have been used to examine the biochemical relationship between the 80-kDa RNase L in healthy control PBMC and the 37-kDa RNase L in PBMC from individuals with CFS. Like the 80-kDa RNase L, the 37-kDa RNase L is present as a catalytically inactive heterodimer complex with the RNase L inhibitor (RLI). Formation of a 37-kDa RNase L-RLI complex indicates that the 37-kDa RNase L is structurally similar to the 80-kDa RNase L at the N-terminus, which contains the 2-5A binding domain. The enzymatically active monomer form of 37-kDa RNase L resolved by 2-D gel electrophoresis has a pI of 6.1. RT-PCR and Southern blot analyses demonstrated that the 37-kDa RNase L is not formed by alternative splicing. In-gel tryptic digestion of the 37-kDa RNase L that was excised from 2-D gels and subsequent MALDI-MS analysis identified three peptide masses that are identical to three predicted peptide masses in the 80-kDa RNase L. The electrophoretic mobility of 2-5A azido photolabeled/immunoprecipitated 37-kDa RNase L was the same under reducing and nonreducing conditions. The results presented show that the 37-kDa form of RNase L in PBMC shares structural and functional features with the native 80-kDa RNase L, in particular in the 2-5A binding and catalytic domains. | D015673 | Fatigue Syndrome, Chronic |
| RNASEL | 19923450 | Distinct antiviral roles for human 2',5'-oligoadenylate synthetase family members against dengue virus infection. | The 2',5'-oligoadenylate synthetase (OAS) and its downstream effector RNase L play important roles in host defense against virus infection. Oas1b, one of the eight Oas1 genes in the mouse genome, has been identified as a murine flavivirus-resistance gene. Four genes, OAS1, OAS2, OAS3, and OAS-like (OASL), have been identified in the human OAS gene family, and 10 isoforms, including OAS1 (p42, p44, p46, p48, and p52), OAS2 (p69 and p71), OAS3 (p100), and OASL (p30 and p59) can be generated by alternative splicing. In this study, we determined the role of the human OAS/RNase L pathway in host defense against dengue virus (DEN) infection and assessed the antiviral potential of each isoform in the human OAS family. DEN replication was reduced by overexpression and enhanced by knockdown of RNase L expression, indicating a protective role for RNase L against DEN replication in human cells. The human OAS1 p42, OAS1 p46, and OAS3 p100, but not the other OAS isoforms, blocked DEN replication via an RNase L-dependent mechanism. Furthermore, the anti-DEN activities of these three OAS isoforms correlated with their ability to trigger RNase L activation in DEN-infected cells. Thus, OAS1 p42/p46 and OAS3 p100 are likely to contribute to host defense against DEN infection and play a role in determining the outcomes of DEN disease severity. | D003715 | Dengue |
Clinically important variants in RNASEL |
| (ClinVar, 04/20/2024) |
| accession_id | uniprot_id | gene_name | Type | Variant | Clinical_significance |
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