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Protein

Probable ATP-dependent RNA helicase DDX58

Gene

DDX58

Organism
Homo sapiens (Human)
Status
Reviewed-Annotation score:

Annotation score:5 out of 5

<p>The annotation score provides a heuristic measure of the annotation content of a UniProtKB entry or proteome. This score <strong>cannot</strong> be used as a measure of the accuracy of the annotation as we cannot define the ‘correct annotation’ for any given protein.<p><a href='/help/annotation_score' target='_top'>More...</a></p>
-Experimental evidence at protein leveli <p>This indicates the type of evidence that supports the existence of the protein. Note that the ‘protein existence’ evidence does not give information on the accuracy or correctness of the sequence(s) displayed.<p><a href='/help/protein_existence' target='_top'>More...</a></p>

<p>This section provides any useful information about the protein, mostly biological knowledge.<p><a href='/help/function_section' target='_top'>More...</a></p>Functioni

Innate immune receptor which acts as a cytoplasmic sensor of viral nucleic acids and plays a major role in sensing viral infection and in the activation of a cascade of antiviral responses including the induction of type I interferons and proinflammatory cytokines. Its ligands include: 5'-triphosphorylated ssRNA and dsRNA and short dsRNA (<1 kb in length). In addition to the 5'-triphosphate moiety, blunt-end base pairing at the 5'-end of the RNA is very essential. Overhangs at the non-triphosphorylated end of the dsRNA RNA have no major impact on its activity. A 3'overhang at the 5'triphosphate end decreases and any 5'overhang at the 5' triphosphate end abolishes its activity. Upon ligand binding it associates with mitochondria antiviral signaling protein (MAVS/IPS1) which activates the IKK-related kinases: TBK1 and IKBKE which phosphorylate interferon regulatory factors: IRF3 and IRF7 which in turn activate transcription of antiviral immunological genes, including interferons (IFNs); IFN-alpha and IFN-beta. Detects both positive and negative strand RNA viruses including members of the families Paramyxoviridae: Human respiratory syncytial virus and measles virus (MeV), Rhabdoviridae: vesicular stomatitis virus (VSV), Orthomyxoviridae: influenza A and B virus, Flaviviridae: Japanese encephalitis virus (JEV), hepatitis C virus (HCV), dengue virus (DENV) and west Nile virus (WNV). It also detects rotavirus and reovirus. Also involved in antiviral signaling in response to viruses containing a dsDNA genome such as Epstein-Barr virus (EBV). Detects dsRNA produced from non-self dsDNA by RNA polymerase III, such as Epstein-Barr virus-encoded RNAs (EBERs). May play important roles in granulocyte production and differentiation, bacterial phagocytosis and in the regulation of cell migration.13 Publications

<p>This subsection of the <a href="http://www.uniprot.org/help/function_section">Function</a> section describes the catalytic activity of an enzyme, i.e. a chemical reaction that the enzyme catalyzes.<p><a href='/help/catalytic_activity' target='_top'>More...</a></p>Catalytic activityi

Sites

Feature keyPosition(s)DescriptionActionsGraphical viewLength
<p>This subsection of the ‘Function’ section indicates at which position the protein binds a given metal ion. The nature of the metal is indicated in the ‘Description’ field.<p><a href='/help/metal' target='_top'>More...</a></p>Metal bindingi810ZincPROSITE-ProRule annotation1
Metal bindingi813ZincPROSITE-ProRule annotation1
Metal bindingi864ZincPROSITE-ProRule annotation1
Metal bindingi869ZincPROSITE-ProRule annotation1

Regions

Feature keyPosition(s)DescriptionActionsGraphical viewLength
<p>This subsection of the ‘Function’ section describes a region in the protein which binds nucleotide phosphates. It always involves more than one amino acid and includes all residues involved in nucleotide-binding.<p><a href='/help/np_bind' target='_top'>More...</a></p>Nucleotide bindingi264 – 271ATPCurated8

<p>The <a href="http://www.geneontology.org/">Gene Ontology (GO)</a> project provides a set of hierarchical controlled vocabulary split into 3 categories:<p><a href='/help/gene_ontology' target='_top'>More...</a></p>GO - Molecular functioni

  • ATP binding Source: UniProtKB-KW
  • double-stranded DNA binding Source: Ensembl
  • double-stranded RNA binding Source: UniProtKB
  • helicase activity Source: UniProtKB-KW
  • identical protein binding Source: IntAct
  • single-stranded RNA binding Source: UniProtKB
  • ubiquitin protein ligase binding Source: UniProtKB
  • zinc ion binding Source: UniProtKB

GO - Biological processi

<p>UniProtKB Keywords constitute a <a href="http://www.uniprot.org/keywords">controlled vocabulary</a> with a hierarchical structure. Keywords summarise the content of a UniProtKB entry and facilitate the search for proteins of interest.<p><a href='/help/keywords' target='_top'>More...</a></p>Keywordsi

Molecular functionHelicase, Hydrolase, RNA-binding
Biological processAntiviral defense, Host-virus interaction, Immunity, Innate immunity
LigandATP-binding, Metal-binding, Nucleotide-binding, Zinc

Enzyme and pathway databases

Reactome - a knowledgebase of biological pathways and processes

More...
Reactomei
R-HSA-1169408 ISG15 antiviral mechanism
R-HSA-168928 DDX58/IFIH1-mediated induction of interferon-alpha/beta
R-HSA-5689880 Ub-specific processing proteases
R-HSA-5689896 Ovarian tumor domain proteases
R-HSA-8983711 OAS antiviral response
R-HSA-918233 TRAF3-dependent IRF activation pathway
R-HSA-933541 TRAF6 mediated IRF7 activation
R-HSA-933542 TRAF6 mediated NF-kB activation
R-HSA-933543 NF-kB activation through FADD/RIP-1 pathway mediated by caspase-8 and -10
R-HSA-936440 Negative regulators of DDX58/IFIH1 signaling

SIGNOR Signaling Network Open Resource

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SIGNORi
O95786

<p>This section provides information about the protein and gene name(s) and synonym(s) and about the organism that is the source of the protein sequence.<p><a href='/help/names_and_taxonomy_section' target='_top'>More...</a></p>Names & Taxonomyi

<p>This subsection of the <a href="http://www.uniprot.org/help/names_and_taxonomy_section">Names and taxonomy</a> section provides an exhaustive list of all names of the protein, from commonly used to obsolete, to allow unambiguous identification of a protein.<p><a href='/help/protein_names' target='_top'>More...</a></p>Protein namesi
Recommended name:
Probable ATP-dependent RNA helicase DDX58 (EC:3.6.4.13)
Alternative name(s):
DEAD box protein 58
RIG-I-like receptor 1
Short name:
RLR-1
Retinoic acid-inducible gene 1 protein
Short name:
RIG-1
Retinoic acid-inducible gene I protein
Short name:
RIG-I
<p>This subsection of the <a href="http://www.uniprot.org/help/names_and_taxonomy_section">Names and taxonomy</a> section indicates the name(s) of the gene(s) that code for the protein sequence(s) described in the entry. Four distinct tokens exist: ‘Name’, ‘Synonyms’, ‘Ordered locus names’ and ‘ORF names’.<p><a href='/help/gene_name' target='_top'>More...</a></p>Gene namesi
Name:DDX58
<p>This subsection of the <a href="http://www.uniprot.org/help/names_and_taxonomy_section">Names and taxonomy</a> section provides information on the name(s) of the organism that is the source of the protein sequence.<p><a href='/help/organism-name' target='_top'>More...</a></p>OrganismiHomo sapiens (Human)
<p>This subsection of the <a href="http://www.uniprot.org/help/names_and_taxonomy_section">Names and taxonomy</a> section shows the unique identifier assigned by the NCBI to the source organism of the protein. This is known as the ‘taxonomic identifier’ or ‘taxid’.<p><a href='/help/taxonomic_identifier' target='_top'>More...</a></p>Taxonomic identifieri9606 [NCBI]
<p>This subsection of the <a href="http://www.uniprot.org/help/names_and_taxonomy_section">Names and taxonomy</a> section contains the taxonomic hierarchical classification lineage of the source organism. It lists the nodes as they appear top-down in the taxonomic tree, with the more general grouping listed first.<p><a href='/help/taxonomic_lineage' target='_top'>More...</a></p>Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
<p>This subsection of the <a href="http://www.uniprot.org/help/names_and_taxonomy_section">Names and taxonomy</a> section is present for entries that are part of a <a href="http://www.uniprot.org/proteomes">proteome</a>, i.e. of a set of proteins thought to be expressed by organisms whose genomes have been completely sequenced.<p><a href='/help/proteomes_manual' target='_top'>More...</a></p>Proteomesi
  • UP000005640 <p>A UniProt <a href="http://www.uniprot.org/manual/proteomes_manual">proteome</a> can consist of several components. <br></br>The component name refers to the genomic component encoding a set of proteins.<p><a href='/help/proteome_component' target='_top'>More...</a></p> Componenti: Chromosome 9

Organism-specific databases

Eukaryotic Pathogen Database Resources

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EuPathDBi
HostDB:ENSG00000107201.9

Human Gene Nomenclature Database

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HGNCi
HGNC:19102 DDX58

Online Mendelian Inheritance in Man (OMIM)

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MIMi
609631 gene

neXtProt; the human protein knowledge platform

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neXtProti
NX_O95786

<p>This section provides information on the location and the topology of the mature protein in the cell.<p><a href='/help/subcellular_location_section' target='_top'>More...</a></p>Subcellular locationi

Extracellular region or secreted Cytosol Plasma membrane Cytoskeleton Lysosome Endosome Peroxisome ER Golgi apparatus Nucleus Mitochondrion Manual annotation Automatic computational assertionGraphics by Christian Stolte; Source: COMPARTMENTS

Keywords - Cellular componenti

Cell junction, Cell membrane, Cell projection, Cytoplasm, Cytoskeleton, Membrane, Tight junction

<p>This section provides information on the disease(s) and phenotype(s) associated with a protein.<p><a href='/help/pathology_and_biotech_section' target='_top'>More...</a></p>Pathology & Biotechi

<p>This subsection of the ‘Pathology and Biotech’ section provides information on the disease(s) associated with genetic variations in a given protein. The information is extracted from the scientific literature and diseases that are also described in the <a href="http://www.ncbi.nlm.nih.gov/sites/entrez?db=omim">OMIM</a> database are represented with a <a href="http://www.uniprot.org/diseases">controlled vocabulary</a> in the following way:<p><a href='/help/involvement_in_disease' target='_top'>More...</a></p>Involvement in diseasei

Singleton-Merten syndrome 2 (SGMRT2)1 Publication
The disease is caused by mutations affecting the gene represented in this entry.
Disease descriptionA form of Singleton-Merten syndrome, an autosomal dominant disorder characterized by marked aortic calcification, dental anomalies, osteopenia, acro-osteolysis, and to a lesser extent glaucoma, psoriasis, muscle weakness, and joint laxity. Additional clinical manifestations include particular facial characteristics and abnormal joint and muscle ligaments. SGMRT2 is an atypical form characterized by variable expression of glaucoma, aortic calcification, and skeletal abnormalities, without dental anomalies.
See also OMIM:616298
Feature keyPosition(s)DescriptionActionsGraphical viewLength
<p>This subsection of the ‘Sequence’ section describes natural variant(s) of the protein sequence.<p><a href='/help/variant' target='_top'>More...</a></p>Natural variantiVAR_073667268C → F in SGMRT2; results in constitutive activation and enhanced interferon-mediated signaling. 1 PublicationCorresponds to variant dbSNP:rs786204848EnsemblClinVar.1
Natural variantiVAR_073668373E → A in SGMRT2; results in constitutive activation and enhanced interferon-mediated signaling. 1 PublicationCorresponds to variant dbSNP:rs786204847EnsemblClinVar.1

Mutagenesis

Feature keyPosition(s)DescriptionActionsGraphical viewLength
<p>This subsection of the <a href="http://www.uniprot.org/manual/pathology_and_biotech_section">'Pathology and Biotech'</a> section describes the effect of the experimental mutation of one or more amino acid(s) on the biological properties of the protein.<p><a href='/help/mutagen' target='_top'>More...</a></p>Mutagenesisi55T → I: No IRF3 signaling activity; no effect on dsRNA binding. 1 Publication1
Mutagenesisi99K → R: Little or no effect on ubiquitination of the 2 CARD domain. Abolishes ubiquitination by RNF125. 2 Publications1
Mutagenesisi154K → R: Reduction of ubiquitination. Reduction of INFB induction. 1 Publication1
Mutagenesisi164K → R: Reduction of ubiquitination. Reduction of INFB induction. 1 Publication1
Mutagenesisi169K → R: Little or no effect on ubiquitination of the 2 CARD domains. 1 Publication1
Mutagenesisi172K → R: Complete loss of ubiquitination; No interaction with MAVS/IPS1; No induction of IFN-beta. 2 Publications1
Mutagenesisi181K → R: Little or no effect on ubiquitination of the 2 CARD domains. 1 Publication1
Mutagenesisi190K → R: Little or no effect on ubiquitination of the 2 CARD domains. 1
Mutagenesisi193K → R: Little or no effect on ubiquitination of the 2 CARD domains. 1 Publication1
Mutagenesisi270K → A: No IRF3 signaling activity. 2 Publications1
Mutagenesisi495N → Q: Complete loss of herpes simplex virus 1 UL37-mediated deamidation; when associated with Q-549. 1 Publication1
Mutagenesisi549N → Q: Complete loss of herpes simplex virus 1 UL37-mediated deamidation; when associated with Q-495. 1 Publication1

Keywords - Diseasei

Disease mutation

Organism-specific databases

DisGeNET

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DisGeNETi
23586

MalaCards human disease database

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MalaCardsi
DDX58
MIMi616298 phenotype

Open Targets

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OpenTargetsi
ENSG00000107201

Orphanet; a database dedicated to information on rare diseases and orphan drugs

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Orphaneti
85191 Singleton-Merten dysplasia

The Pharmacogenetics and Pharmacogenomics Knowledge Base

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PharmGKBi
PA134994272

Polymorphism and mutation databases

BioMuta curated single-nucleotide variation and disease association database

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BioMutai
DDX58

<p>This section describes post-translational modifications (PTMs) and/or processing events.<p><a href='/help/ptm_processing_section' target='_top'>More...</a></p>PTM / Processingi

Molecule processing

Feature keyPosition(s)DescriptionActionsGraphical viewLength
<p>This subsection of the ‘PTM / Processing’ section describes the extent of a polypeptide chain in the mature protein following processing.<p><a href='/help/chain' target='_top'>More...</a></p>ChainiPRO_00001440931 – 925Probable ATP-dependent RNA helicase DDX58Add BLAST925

Amino acid modifications

Feature keyPosition(s)DescriptionActionsGraphical viewLength
<p>This subsection of the <a href="http://www.uniprot.org/help/ptm_processing_section">PTM / Processing</a> section describes <strong>covalent linkages</strong> of various types formed <strong>between two proteins (interchain cross-links)</strong> or <strong>between two parts of the same protein (intrachain cross-links)</strong>, except the disulfide bonds that are annotated in the <a href="http://www.uniprot.org/manual/disulfid">'Disulfide bond'</a> subsection.<p><a href='/help/crosslnk' target='_top'>More...</a></p>Cross-linki154Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin)1 Publication
Cross-linki164Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin)1 Publication
Cross-linki172Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin)1 Publication
Cross-linki181Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin)1 Publication
<p>This subsection of the ‘PTM / Processing’ section specifies the position and type of each modified residue excluding <a href="http://www.uniprot.org/manual/lipid">lipids</a>, <a href="http://www.uniprot.org/manual/carbohyd">glycans</a> and <a href="http://www.uniprot.org/manual/crosslnk">protein cross-links</a>.<p><a href='/help/mod_res' target='_top'>More...</a></p>Modified residuei495(Microbial infection) Deamidated asparagine; by herpes simplex virus 1/HHV-1 UL371 Publication1
Modified residuei549(Microbial infection) Deamidated asparagine; by herpes simplex virus 1/HHV-1 UL371 Publication1
Modified residuei770Phosphothreonine; by CK21 Publication1
Cross-linki812Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin)By similarity
Modified residuei854Phosphoserine; by CK21 Publication1
Modified residuei855Phosphoserine; by CK21 Publication1
Modified residuei858N6-acetyllysineCombined sources1

<p>This subsection of the <a href="http://www.uniprot.org/help/ptm_processing_section">PTM/processing</a> section describes post-translational modifications (PTMs). This subsection <strong>complements</strong> the information provided at the sequence level or describes modifications for which <strong>position-specific data is not yet available</strong>.<p><a href='/help/post-translational_modification' target='_top'>More...</a></p>Post-translational modificationi

(Microbial infection) Deamidated on 'Asn-495' and 'Asn-549' by herpes simplex virus 1 protein UL37. These modifications eliminate DDX58 detection of viral RNA and restriction of viral replication.1 Publication
Phosphorylated in resting cells and dephosphorylated in RNA virus-infected cells. Phosphorylation at Thr-770, Ser-854 and Ser-855 results in inhibition of its activity while dephosphorylation at these sites results in its activation.1 Publication
ISGylated. Conjugated to ubiquitin-like protein ISG15 upon IFN-beta stimulation. ISGylation negatively regulates its function in antiviral signaling response.3 Publications
Sumoylated, probably by MUL1; inhibiting its polyubiquitination.2 Publications
Ubiquitinated. Undergoes 'Lys-48'- and 'Lys-63'-linked ubiquitination. Lys-172 is the critical site for TRIM25-mediated ubiquitination, for MAVS/IPS1 binding and to induce anti-viral signal transduction (PubMed:17392790, PubMed:30193849). Lys-154, Lys-164 and Lys-172 are critical sites for RNF135-mediated and TRIM4-mediated ubiquitination (PubMed:19017631, PubMed:19484123, PubMed:24755855). Deubiquitinated by CYLD, a protease that selectively cleaves 'Lys-63'-linked ubiquitin chains (PubMed:18636086). Also probably deubiquitinated by USP17L2/USP17 that cleaves 'Lys-48'-and 'Lys-63'-linked ubiquitin chains and positively regulates the receptor (PubMed:20368735). Ubiquitinated at Lys-181 by RNF125, leading to its degradation: ubiquitination takes place upon viral infection and is enhanced 'Lys-63'-linked ubiquitination of the CARD domains, which promote interaction with VCP/p97 and subsequent recruitment of RNF125 (PubMed:17460044, PubMed:26471729). Ubiquitinated at Lys-812 by CBL, leading to its degradation: ubiquitination takes place upon viral infection and involves 'Lys-48'-linked ubiquitination (By similarity).By similarity9 Publications

Keywords - PTMi

Acetylation, Isopeptide bond, Phosphoprotein, Ubl conjugation

Proteomic databases

Encyclopedia of Proteome Dynamics

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EPDi
O95786

jPOST - Japan Proteome Standard Repository/Database

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jPOSTi
O95786

MaxQB - The MaxQuant DataBase

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MaxQBi
O95786

PaxDb, a database of protein abundance averages across all three domains of life

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PaxDbi
O95786

PeptideAtlas

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PeptideAtlasi
O95786

PRoteomics IDEntifications database

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PRIDEi
O95786

ProteomicsDB human proteome resource

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ProteomicsDBi
51047
51048 [O95786-2]

PTM databases

iPTMnet integrated resource for PTMs in systems biology context

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iPTMneti
O95786

Comprehensive resource for the study of protein post-translational modifications (PTMs) in human, mouse and rat.

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PhosphoSitePlusi
O95786

<p>This section provides information on the expression of a gene at the mRNA or protein level in cells or in tissues of multicellular organisms.<p><a href='/help/expression_section' target='_top'>More...</a></p>Expressioni

<p>This subsection of the ‘Expression’ section provides information on the expression of a gene at the mRNA or protein level in cells or in tissues of multicellular organisms. By default, the information is derived from experiments at the mRNA level, unless specified ‘at protein level’. <br></br>Examples: <a href="http://www.uniprot.org/uniprot/P92958#expression">P92958</a>, <a href="http://www.uniprot.org/uniprot/Q8TDN4#expression">Q8TDN4</a>, <a href="http://www.uniprot.org/uniprot/O14734#expression">O14734</a><p><a href='/help/tissue_specificity' target='_top'>More...</a></p>Tissue specificityi

Present in vascular smooth cells (at protein level).1 Publication

<p>This subsection of the ‘Expression’ section reports the experimentally proven effects of inducers and repressors (usually chemical compounds or environmental factors) on the level of protein (or mRNA) expression (up-regulation, down-regulation, constitutive expression).<p><a href='/help/induction' target='_top'>More...</a></p>Inductioni

By bacterial lipopolysaccharides (LPS) in endothelial cells. By interferon (IFN).5 Publications

Gene expression databases

Bgee dataBase for Gene Expression Evolution

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Bgeei
ENSG00000107201 Expressed in 216 organ(s), highest expression level in buccal mucosa cell

CleanEx database of gene expression profiles

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CleanExi
HS_DDX58

ExpressionAtlas, Differential and Baseline Expression

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ExpressionAtlasi
O95786 baseline and differential

Genevisible search portal to normalized and curated expression data from Genevestigator

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Genevisiblei
O95786 HS

Organism-specific databases

Human Protein Atlas

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HPAi
CAB012643
HPA047193

<p>This section provides information on the quaternary structure of a protein and on interaction(s) with other proteins or protein complexes.<p><a href='/help/interaction_section' target='_top'>More...</a></p>Interactioni

<p>This subsection of the <a href="http://www.uniprot.org/help/interaction_section">'Interaction'</a> section provides information about the protein quaternary structure and interaction(s) with other proteins or protein complexes (with the exception of physiological receptor-ligand interactions which are annotated in the <a href="http://www.uniprot.org/help/function_section">'Function'</a> section).<p><a href='/help/subunit_structure' target='_top'>More...</a></p>Subunit structurei

Monomer; maintained as a monomer in an autoinhibited state. Upon viral dsRNA binding and conformation shift, homomultimerizes and interacts (via tandem CARD domain) with MAVS/IPS1 promoting its filamentation. Interacts with DHX58/LGP2, IKBKE, TBK1 and TMEM173/STING. Interacts (via CARD domain) with TRIM25 (via SPRY domain). Interacts with RNF135. Interacts with CYLD. Interacts with NLRC5; blocks the interaction of MAVS/IPS1 to DDX58. Interacts with SRC. Interacts with DDX60. Interacts with isoform 2 of ZC3HAV1 (via zinc-fingers) in an RNA-dependent manner. Interacts (via tandem CARD domain) with SEC14L1; the interaction is direct and impairs the interaction of DDX58 with MAVS/IPS1. Interacts with VCP/p97; interaction is direct and leads to recruit RNF125 and subsequent ubiquitination and degradation (PubMed:26471729). Interacts with NOP53; may regulate DDX58 through USP15-mediated 'Lys-63'-linked deubiquitination (PubMed:27824081). Interacts with LRRC25 (PubMed:29288164). Interacts with ZCCHC3; leading to activate DDX58/RIG-I (PubMed:30193849).22 Publications
(Microbial infection) Interacts with protein Z of Guanarito virus, Machupo virus, Junin arenavirus and Sabia virus. This interaction disrupts its interaction with MAVS/IPS1, impeding downstream IRF3 and NF-kappa-B activation and resulting in decreased IFN-beta induction (PubMed:20007272).1 Publication
(Microbial infection) Interacts (via CARD domain) with Human respiratory syncytial virus A non-structural protein 2 (NS2) and this interaction disrupts its interaction with MAVS/IPS1, impeding downstream IRF3 activation (PubMed:19193793).1 Publication
(Microbial infection) Interacts with Rotavirus A non-structural protein 1 (NSP1) and this interaction induces down-regulation of DDX58/RIG-I (PubMed:22152002).1 Publication
(Microbial infection) Interacts with herpes simplex virus 1 protein US11; this interaction prevents the interaction of MAVS/IPS1 to DDX58 (PubMed:22301138).1 Publication
(Microbial infection) Interacts with herpes simplex virus 1 protein UL37; this interaction daeminates DDX58 and inhibits its activation.1 Publication

<p>This subsection of the '<a href="http://www.uniprot.org/help/interaction_section%27">Interaction</a> section provides information about binary protein-protein interactions. The data presented in this section are a quality-filtered subset of binary interactions automatically derived from the <a href="http://www.ebi.ac.uk/intact/">IntAct database</a>. It is updated on a monthly basis. Each binary interaction is displayed on a separate line.<p><a href='/help/binary_interactions' target='_top'>More...</a></p>Binary interactionsi

GO - Molecular functioni

Protein-protein interaction databases

The Biological General Repository for Interaction Datasets (BioGrid)

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BioGridi
117121, 51 interactors

CORUM comprehensive resource of mammalian protein complexes

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CORUMi
O95786

Database of interacting proteins

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DIPi
DIP-35444N

Protein interaction database and analysis system

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IntActi
O95786, 32 interactors

Molecular INTeraction database

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MINTi
O95786

STRING: functional protein association networks

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STRINGi
9606.ENSP00000369213

<p>This section provides information on the tertiary and secondary structure of a protein.<p><a href='/help/structure_section' target='_top'>More...</a></p>Structurei

Secondary structure

1925
Legend: HelixTurnBeta strandPDB Structure known for this area
Show more details

3D structure databases

Select the link destinations:

Protein Data Bank Europe

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PDBei

Protein Data Bank RCSB

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RCSB PDBi

Protein Data Bank Japan

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PDBji
Links Updated
PDB entryMethodResolution (Å)ChainPositionsPDBsum
2LWDNMR-A95-190[»]
2LWENMR-A95-190[»]
2QFBX-ray3.00A/B/C/D/E/F/G/H/I/J802-925[»]
2QFDX-ray2.70A/B/C/D/E/F/G/H/I/J802-925[»]
2RMJNMR-A792-925[»]
2YKGX-ray2.50A230-925[»]
3LRNX-ray2.60A/B803-923[»]
3LRRX-ray2.15A/B803-923[»]
3NCUX-ray2.55A/B792-925[»]
3OG8X-ray2.40A/B802-925[»]
3ZD6X-ray2.80A230-925[»]
3ZD7X-ray2.50A230-925[»]
4AY2X-ray2.80A239-925[»]
4BPBX-ray2.58A230-925[»]
4NQKX-ray3.70A/B/C/D1-200[»]
4ON9X-ray2.71A/B230-793[»]
4P4HX-ray3.40A/B/C/D/E/F/G/H1-201[»]
5E3HX-ray2.70A232-925[»]
5F98X-ray3.28A/C/E/G/I/K232-925[»]
5F9FX-ray2.60A/C/E/G/I/K232-925[»]
5F9HX-ray3.10A/C/E/G/I/K232-925[»]
6GPGX-ray2.89A232-925[»]

Protein Model Portal of the PSI-Nature Structural Biology Knowledgebase

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ProteinModelPortali
O95786

SWISS-MODEL Repository - a database of annotated 3D protein structure models

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SMRi
O95786

Database of comparative protein structure models

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ModBasei
Search...

MobiDB: a database of protein disorder and mobility annotations

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MobiDBi
Search...

Miscellaneous databases

Relative evolutionary importance of amino acids within a protein sequence

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EvolutionaryTracei
O95786

<p>This section provides information on sequence similarities with other proteins and the domain(s) present in a protein.<p><a href='/help/family_and_domains_section' target='_top'>More...</a></p>Family & Domainsi

Domains and Repeats

Feature keyPosition(s)DescriptionActionsGraphical viewLength
<p>This subsection of the <a href="http://www.uniprot.org/help/family_and_domains_section">Family and Domains</a> section describes the position and type of a domain, which is defined as a specific combination of secondary structures organized into a characteristic three-dimensional structure or fold.<p><a href='/help/domain' target='_top'>More...</a></p>Domaini1 – 87CARD 1Add BLAST87
Domaini92 – 172CARD 2Add BLAST81
Domaini251 – 430Helicase ATP-bindingPROSITE-ProRule annotationAdd BLAST180
Domaini610 – 776Helicase C-terminalPROSITE-ProRule annotationAdd BLAST167
Domaini794 – 925RLR CTRPROSITE-ProRule annotationAdd BLAST132

Region

Feature keyPosition(s)DescriptionActionsGraphical viewLength
<p>This subsection of the ‘Family and Domains’ section describes a region of interest that cannot be described in other subsections.<p><a href='/help/region' target='_top'>More...</a></p>Regioni218 – 925Interaction with ZC3HAV11 PublicationAdd BLAST708

Motif

Feature keyPosition(s)DescriptionActionsGraphical viewLength
<p>This subsection of the ‘Family and Domains’ section describes a short (usually not more than 20 amino acids) conserved sequence motif of biological significance.<p><a href='/help/motif' target='_top'>More...</a></p>Motifi372 – 375DECH box4

<p>This subsection of the ‘Family and domains’ section provides general information on the biological role of a domain. The term ‘domain’ is intended here in its wide acceptation, it may be a structural domain, a transmembrane region or a functional domain. Several domains are described in this subsection.<p><a href='/help/domain_cc' target='_top'>More...</a></p>Domaini

The RLR CTR domain controls homomultimerization and interaction with MAVS/IPS1. In the absence of viral infection, the protein is maintained as a monomer in an autoinhibited state with the CARD domains masked through intramolecular interactions mediated by the RLR CTR domain. Upon binding to viral RNA in the presence of ATP, the RLR CTR domain induces a conformational change exposing the CARD domain and promotes dimerization and CARD interactions with the adapter protein MAVS/IPS1 leading to the induction of downstream signaling.
The helicase domain is responsible for dsRNA recognition.
The 2 CARD domains are responsible for interaction with and signaling through MAVS/IPS1 and for association with the actin cytoskeleton.
The second CARD domain is the primary site for 'Lys-63'-linked ubiquitination.1 Publication

<p>This subsection of the ‘Family and domains’ section provides information about the sequence similarity with other proteins.<p><a href='/help/sequence_similarities' target='_top'>More...</a></p>Sequence similaritiesi

Belongs to the helicase family. RLR subfamily.Curated

Keywords - Domaini

Repeat

Phylogenomic databases

evolutionary genealogy of genes: Non-supervised Orthologous Groups

More...
eggNOGi
KOG0354 Eukaryota
COG1111 LUCA

Ensembl GeneTree

More...
GeneTreei
ENSGT00940000153173

The HOGENOM Database of Homologous Genes from Fully Sequenced Organisms

More...
HOGENOMi
HOG000230911

The HOVERGEN Database of Homologous Vertebrate Genes

More...
HOVERGENi
HBG052325

InParanoid: Eukaryotic Ortholog Groups

More...
InParanoidi
O95786

KEGG Orthology (KO)

More...
KOi
K12646

Identification of Orthologs from Complete Genome Data

More...
OMAi
LISQECE

Database of Orthologous Groups

More...
OrthoDBi
1337630at2759

Database for complete collections of gene phylogenies

More...
PhylomeDBi
O95786

TreeFam database of animal gene trees

More...
TreeFami
TF330258

Family and domain databases

Conserved Domains Database

More...
CDDi
cd00079 HELICc, 1 hit

Gene3D Structural and Functional Annotation of Protein Families

More...
Gene3Di
2.170.150.30, 1 hit

Integrated resource of protein families, domains and functional sites

More...
InterProi
View protein in InterPro
IPR031964 CARD_dom
IPR011545 DEAD/DEAH_box_helicase_dom
IPR014001 Helicase_ATP-bd
IPR001650 Helicase_C
IPR027417 P-loop_NTPase
IPR038557 RLR_C_sf
IPR021673 RLR_CTR

Pfam protein domain database

More...
Pfami
View protein in Pfam
PF16739 CARD_2, 2 hits
PF00270 DEAD, 1 hit
PF00271 Helicase_C, 1 hit
PF11648 RIG-I_C-RD, 1 hit

Simple Modular Architecture Research Tool; a protein domain database

More...
SMARTi
View protein in SMART
SM00487 DEXDc, 1 hit
SM00490 HELICc, 1 hit

Superfamily database of structural and functional annotation

More...
SUPFAMi
SSF52540 SSF52540, 2 hits

PROSITE; a protein domain and family database

More...
PROSITEi
View protein in PROSITE
PS51192 HELICASE_ATP_BIND_1, 1 hit
PS51194 HELICASE_CTER, 1 hit
PS51789 RLR_CTR, 1 hit

<p>This section displays by default the canonical protein sequence and upon request all isoforms described in the entry. It also includes information pertinent to the sequence(s), including <a href="http://www.uniprot.org/help/sequence_length">length</a> and <a href="http://www.uniprot.org/help/sequences">molecular weight</a>.<p><a href='/help/sequences_section' target='_top'>More...</a></p>Sequences (2+)i

<p>This subsection of the <a href="http://www.uniprot.org/help/sequences_section">Sequence</a> section indicates if the <a href="http://www.uniprot.org/help/canonical_and_isoforms">canonical sequence</a> displayed by default in the entry is complete or not.<p><a href='/help/sequence_status' target='_top'>More...</a></p>Sequence statusi: Complete.

This entry describes 2 <p>This subsection of the ‘Sequence’ section lists the alternative protein sequences (isoforms) that can be generated from the same gene by a single or by the combination of up to four biological events (alternative promoter usage, alternative splicing, alternative initiation and ribosomal frameshifting). Additionally, this section gives relevant information on each alternative protein isoform.<p><a href='/help/alternative_products' target='_top'>More...</a></p> isoformsi produced by alternative splicing. AlignAdd to basket

This entry has 2 described isoforms and 1 potential isoform that is computationally mapped.Show allAlign All

Isoform 1 (identifier: O95786-1) [UniParc]FASTAAdd to basket

This isoform has been chosen as the 'canonical' sequence. All positional information in this entry refers to it. This is also the sequence that appears in the downloadable versions of the entry.

« Hide
        10         20         30         40         50
MTTEQRRSLQ AFQDYIRKTL DPTYILSYMA PWFREEEVQY IQAEKNNKGP
60 70 80 90 100
MEAATLFLKF LLELQEEGWF RGFLDALDHA GYSGLYEAIE SWDFKKIEKL
110 120 130 140 150
EEYRLLLKRL QPEFKTRIIP TDIISDLSEC LINQECEEIL QICSTKGMMA
160 170 180 190 200
GAEKLVECLL RSDKENWPKT LKLALEKERN KFSELWIVEK GIKDVETEDL
210 220 230 240 250
EDKMETSDIQ IFYQEDPECQ NLSENSCPPS EVSDTNLYSP FKPRNYQLEL
260 270 280 290 300
ALPAMKGKNT IICAPTGCGK TFVSLLICEH HLKKFPQGQK GKVVFFANQI
310 320 330 340 350
PVYEQQKSVF SKYFERHGYR VTGISGATAE NVPVEQIVEN NDIIILTPQI
360 370 380 390 400
LVNNLKKGTI PSLSIFTLMI FDECHNTSKQ HPYNMIMFNY LDQKLGGSSG
410 420 430 440 450
PLPQVIGLTA SVGVGDAKNT DEALDYICKL CASLDASVIA TVKHNLEELE
460 470 480 490 500
QVVYKPQKFF RKVESRISDK FKYIIAQLMR DTESLAKRIC KDLENLSQIQ
510 520 530 540 550
NREFGTQKYE QWIVTVQKAC MVFQMPDKDE ESRICKALFL YTSHLRKYND
560 570 580 590 600
ALIISEHARM KDALDYLKDF FSNVRAAGFD EIEQDLTQRF EEKLQELESV
610 620 630 640 650
SRDPSNENPK LEDLCFILQE EYHLNPETIT ILFVKTRALV DALKNWIEGN
660 670 680 690 700
PKLSFLKPGI LTGRGKTNQN TGMTLPAQKC ILDAFKASGD HNILIATSVA
710 720 730 740 750
DEGIDIAQCN LVILYEYVGN VIKMIQTRGR GRARGSKCFL LTSNAGVIEK
760 770 780 790 800
EQINMYKEKM MNDSILRLQT WDEAVFREKI LHIQTHEKFI RDSQEKPKPV
810 820 830 840 850
PDKENKKLLC RKCKALACYT ADVRVIEECH YTVLGDAFKE CFVSRPHPKP
860 870 880 890 900
KQFSSFEKRA KIFCARQNCS HDWGIHVKYK TFEIPVIKIE SFVVEDIATG
910 920
VQTLYSKWKD FHFEKIPFDP AEMSK
Length:925
Mass (Da):106,600
Last modified:November 8, 2005 - v2
<p>The checksum is a form of redundancy check that is calculated from the sequence. It is useful for tracking sequence updates.</p> <p>It should be noted that while, in theory, two different sequences could have the same checksum value, the likelihood that this would happen is extremely low.</p> <p>However UniProtKB may contain entries with identical sequences in case of multiple genes (paralogs).</p> <p>The checksum is computed as the sequence 64-bit Cyclic Redundancy Check value (CRC64) using the generator polynomial: x<sup>64</sup> + x<sup>4</sup> + x<sup>3</sup> + x + 1. The algorithm is described in the ISO 3309 standard. </p> <p class="publication">Press W.H., Flannery B.P., Teukolsky S.A. and Vetterling W.T.<br /> <strong>Cyclic redundancy and other checksums</strong><br /> <a href="http://www.nrbook.com/b/bookcpdf.php">Numerical recipes in C 2nd ed., pp896-902, Cambridge University Press (1993)</a>)</p> Checksum:iBF0D501C395BAE25
GO
Isoform 2 (identifier: O95786-2) [UniParc]FASTAAdd to basket

The sequence of this isoform differs from the canonical sequence as follows:
     36-80: Missing.

Note: No experimental confirmation available.
Show »
Length:880
Mass (Da):101,377
Checksum:i4B1603B6F2F37A66
GO

<p>In eukaryotic reference proteomes, unreviewed entries that are likely to belong to the same gene are computationally mapped, based on gene identifiers from Ensembl, EnsemblGenomes and model organism databases.<p><a href='/help/gene_centric_isoform_mapping' target='_top'>More...</a></p>Computationally mapped potential isoform sequencesi

There is 1 potential isoform mapped to this entry.BLASTAlignShow allAdd to basket
EntryEntry nameProtein names
Gene namesLengthAnnotation
A2A376A2A376_HUMAN
Probable ATP-dependent RNA helicase...
DDX58
722Annotation score:

Annotation score:2 out of 5

<p>The annotation score provides a heuristic measure of the annotation content of a UniProtKB entry or proteome. This score <strong>cannot</strong> be used as a measure of the accuracy of the annotation as we cannot define the ‘correct annotation’ for any given protein.<p><a href='/help/annotation_score' target='_top'>More...</a></p>

Natural variant

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Natural variantiVAR_0237477R → C1 PublicationCorresponds to variant dbSNP:rs10813831Ensembl.1
Natural variantiVAR_073667268C → F in SGMRT2; results in constitutive activation and enhanced interferon-mediated signaling. 1 PublicationCorresponds to variant dbSNP:rs786204848EnsemblClinVar.1
Natural variantiVAR_073668373E → A in SGMRT2; results in constitutive activation and enhanced interferon-mediated signaling. 1 PublicationCorresponds to variant dbSNP:rs786204847EnsemblClinVar.1
Natural variantiVAR_023748580D → E2 PublicationsCorresponds to variant dbSNP:rs17217280Ensembl.1

Alternative sequence

Feature keyPosition(s)DescriptionActionsGraphical viewLength
<p>This subsection of the ‘Sequence’ section describes the sequence of naturally occurring alternative protein isoform(s). The changes in the amino acid sequence may be due to alternative splicing, alternative promoter usage, alternative initiation, or ribosomal frameshifting. The information stored in this subsection is used to automatically construct alternative protein sequence(s) for display.<p><a href='/help/var_seq' target='_top'>More...</a></p>Alternative sequenceiVSP_01605436 – 80Missing in isoform 2. 1 PublicationAdd BLAST45

Sequence databases

Select the link destinations:

EMBL nucleotide sequence database

More...
EMBLi

GenBank nucleotide sequence database

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GenBanki

DNA Data Bank of Japan; a nucleotide sequence database

More...
DDBJi
Links Updated
AF038963 mRNA Translation: AAD19826.1
AL161783 Genomic DNA No translation available.
AL353671 Genomic DNA No translation available.
CH471071 Genomic DNA Translation: EAW58548.1
BC132786 mRNA Translation: AAI32787.1
BC136610 mRNA Translation: AAI36611.1
BX647917 mRNA Translation: CAI46068.1
AL137608 mRNA Translation: CAB70840.1

The Consensus CDS (CCDS) project

More...
CCDSi
CCDS6526.1 [O95786-1]

Protein sequence database of the Protein Information Resource

More...
PIRi
T46312

NCBI Reference Sequences

More...
RefSeqi
NP_055129.2, NM_014314.3 [O95786-1]

UniGene gene-oriented nucleotide sequence clusters

More...
UniGenei
Hs.190622

Genome annotation databases

Ensembl eukaryotic genome annotation project

More...
Ensembli
ENST00000379883; ENSP00000369213; ENSG00000107201 [O95786-1]

Database of genes from NCBI RefSeq genomes

More...
GeneIDi
23586

KEGG: Kyoto Encyclopedia of Genes and Genomes

More...
KEGGi
hsa:23586

UCSC genome browser

More...
UCSCi
uc003zra.4 human [O95786-1]

Keywords - Coding sequence diversityi

Alternative splicing, Polymorphism

<p>This section provides links to proteins that are similar to the protein sequence(s) described in this entry at different levels of sequence identity thresholds (100%, 90% and 50%) based on their membership in UniProt Reference Clusters (<a href="http://www.uniprot.org/help/uniref">UniRef</a>).<p><a href='/help/similar_proteins_section' target='_top'>More...</a></p>Similar proteinsi

<p>This section is used to point to information related to entries and found in data collections other than UniProtKB.<p><a href='/help/cross_references_section' target='_top'>More...</a></p>Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AF038963 mRNA Translation: AAD19826.1
AL161783 Genomic DNA No translation available.
AL353671 Genomic DNA No translation available.
CH471071 Genomic DNA Translation: EAW58548.1
BC132786 mRNA Translation: AAI32787.1
BC136610 mRNA Translation: AAI36611.1
BX647917 mRNA Translation: CAI46068.1
AL137608 mRNA Translation: CAB70840.1
CCDSiCCDS6526.1 [O95786-1]
PIRiT46312
RefSeqiNP_055129.2, NM_014314.3 [O95786-1]
UniGeneiHs.190622

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
PDB entryMethodResolution (Å)ChainPositionsPDBsum
2LWDNMR-A95-190[»]
2LWENMR-A95-190[»]
2QFBX-ray3.00A/B/C/D/E/F/G/H/I/J802-925[»]
2QFDX-ray2.70A/B/C/D/E/F/G/H/I/J802-925[»]
2RMJNMR-A792-925[»]
2YKGX-ray2.50A230-925[»]
3LRNX-ray2.60A/B803-923[»]
3LRRX-ray2.15A/B803-923[»]
3NCUX-ray2.55A/B792-925[»]
3OG8X-ray2.40A/B802-925[»]
3ZD6X-ray2.80A230-925[»]
3ZD7X-ray2.50A230-925[»]
4AY2X-ray2.80A239-925[»]
4BPBX-ray2.58A230-925[»]
4NQKX-ray3.70A/B/C/D1-200[»]
4ON9X-ray2.71A/B230-793[»]
4P4HX-ray3.40A/B/C/D/E/F/G/H1-201[»]
5E3HX-ray2.70A232-925[»]
5F98X-ray3.28A/C/E/G/I/K232-925[»]
5F9FX-ray2.60A/C/E/G/I/K232-925[»]
5F9HX-ray3.10A/C/E/G/I/K232-925[»]
6GPGX-ray2.89A232-925[»]
ProteinModelPortaliO95786
SMRiO95786
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi117121, 51 interactors
CORUMiO95786
DIPiDIP-35444N
IntActiO95786, 32 interactors
MINTiO95786
STRINGi9606.ENSP00000369213

PTM databases

iPTMnetiO95786
PhosphoSitePlusiO95786

Polymorphism and mutation databases

BioMutaiDDX58

Proteomic databases

EPDiO95786
jPOSTiO95786
MaxQBiO95786
PaxDbiO95786
PeptideAtlasiO95786
PRIDEiO95786
ProteomicsDBi51047
51048 [O95786-2]

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsembliENST00000379883; ENSP00000369213; ENSG00000107201 [O95786-1]
GeneIDi23586
KEGGihsa:23586
UCSCiuc003zra.4 human [O95786-1]

Organism-specific databases

Comparative Toxicogenomics Database

More...
CTDi
23586
DisGeNETi23586
EuPathDBiHostDB:ENSG00000107201.9

GeneCards: human genes, protein and diseases

More...
GeneCardsi
DDX58
HGNCiHGNC:19102 DDX58
HPAiCAB012643
HPA047193
MalaCardsiDDX58
MIMi609631 gene
616298 phenotype
neXtProtiNX_O95786
OpenTargetsiENSG00000107201
Orphaneti85191 Singleton-Merten dysplasia
PharmGKBiPA134994272

GenAtlas: human gene database

More...
GenAtlasi
Search...

Phylogenomic databases

eggNOGiKOG0354 Eukaryota
COG1111 LUCA
GeneTreeiENSGT00940000153173
HOGENOMiHOG000230911
HOVERGENiHBG052325
InParanoidiO95786
KOiK12646
OMAiLISQECE
OrthoDBi1337630at2759
PhylomeDBiO95786
TreeFamiTF330258

Enzyme and pathway databases

ReactomeiR-HSA-1169408 ISG15 antiviral mechanism
R-HSA-168928 DDX58/IFIH1-mediated induction of interferon-alpha/beta
R-HSA-5689880 Ub-specific processing proteases
R-HSA-5689896 Ovarian tumor domain proteases
R-HSA-8983711 OAS antiviral response
R-HSA-918233 TRAF3-dependent IRF activation pathway
R-HSA-933541 TRAF6 mediated IRF7 activation
R-HSA-933542 TRAF6 mediated NF-kB activation
R-HSA-933543 NF-kB activation through FADD/RIP-1 pathway mediated by caspase-8 and -10
R-HSA-936440 Negative regulators of DDX58/IFIH1 signaling
SIGNORiO95786

Miscellaneous databases

ChiTaRS: a database of human, mouse and fruit fly chimeric transcripts and RNA-sequencing data

More...
ChiTaRSi
DDX58 human
EvolutionaryTraceiO95786

The Gene Wiki collection of pages on human genes and proteins

More...
GeneWikii
RIG-I

Database of phenotypes from RNA interference screens in Drosophila and Homo sapiens

More...
GenomeRNAii
23586

Protein Ontology

More...
PROi
PR:O95786

The Stanford Online Universal Resource for Clones and ESTs

More...
SOURCEi
Search...

Gene expression databases

BgeeiENSG00000107201 Expressed in 216 organ(s), highest expression level in buccal mucosa cell
CleanExiHS_DDX58
ExpressionAtlasiO95786 baseline and differential
GenevisibleiO95786 HS

Family and domain databases

CDDicd00079 HELICc, 1 hit
Gene3Di2.170.150.30, 1 hit
InterProiView protein in InterPro
IPR031964 CARD_dom
IPR011545 DEAD/DEAH_box_helicase_dom
IPR014001 Helicase_ATP-bd
IPR001650 Helicase_C
IPR027417 P-loop_NTPase
IPR038557 RLR_C_sf
IPR021673 RLR_CTR
PfamiView protein in Pfam
PF16739 CARD_2, 2 hits
PF00270 DEAD, 1 hit
PF00271 Helicase_C, 1 hit
PF11648 RIG-I_C-RD, 1 hit
SMARTiView protein in SMART
SM00487 DEXDc, 1 hit
SM00490 HELICc, 1 hit
SUPFAMiSSF52540 SSF52540, 2 hits
PROSITEiView protein in PROSITE
PS51192 HELICASE_ATP_BIND_1, 1 hit
PS51194 HELICASE_CTER, 1 hit
PS51789 RLR_CTR, 1 hit

ProtoNet; Automatic hierarchical classification of proteins

More...
ProtoNeti
Search...

<p>This section provides general information on the entry.<p><a href='/help/entry_information_section' target='_top'>More...</a></p>Entry informationi

<p>This subsection of the ‘Entry information’ section provides a mnemonic identifier for a UniProtKB entry, but it is not a stable identifier. Each reviewed entry is assigned a unique entry name upon integration into UniProtKB/Swiss-Prot.<p><a href='/help/entry_name' target='_top'>More...</a></p>Entry nameiDDX58_HUMAN
<p>This subsection of the ‘Entry information’ section provides one or more accession number(s). These are stable identifiers and should be used to cite UniProtKB entries. Upon integration into UniProtKB, each entry is assigned a unique accession number, which is called ‘Primary (citable) accession number’.<p><a href='/help/accession_numbers' target='_top'>More...</a></p>AccessioniPrimary (citable) accession number: O95786
Secondary accession number(s): A2RU81
, Q5HYE1, Q5VYT1, Q9NT04
<p>This subsection of the ‘Entry information’ section shows the date of integration of the entry into UniProtKB, the date of the last sequence update and the date of the last annotation modification (‘Last modified’). The version number for both the entry and the <a href="http://www.uniprot.org/help/canonical_and_isoforms">canonical sequence</a> are also displayed.<p><a href='/help/entry_history' target='_top'>More...</a></p>Entry historyiIntegrated into UniProtKB/Swiss-Prot: November 8, 2005
Last sequence update: November 8, 2005
Last modified: January 16, 2019
This is version 167 of the entry and version 2 of the sequence. See complete history.
<p>This subsection of the ‘Entry information’ section indicates whether the entry has been manually annotated and reviewed by UniProtKB curators or not, in other words, if the entry belongs to the Swiss-Prot section of UniProtKB (<strong>reviewed</strong>) or to the computer-annotated TrEMBL section (<strong>unreviewed</strong>).<p><a href='/help/entry_status' target='_top'>More...</a></p>Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program
DisclaimerAny medical or genetic information present in this entry is provided for research, educational and informational purposes only. It is not in any way intended to be used as a substitute for professional medical advice, diagnosis, treatment or care.

<p>This section contains any relevant information that doesn’t fit in any other defined sections<p><a href='/help/miscellaneous_section' target='_top'>More...</a></p>Miscellaneousi

Keywords - Technical termi

3D-structure, Complete proteome, Reference proteome

Documents

  1. SIMILARITY comments
    Index of protein domains and families
  2. Human chromosome 9
    Human chromosome 9: entries, gene names and cross-references to MIM
  3. Human polymorphisms and disease mutations
    Index of human polymorphisms and disease mutations
  4. MIM cross-references
    Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot
  5. PDB cross-references
    Index of Protein Data Bank (PDB) cross-references
  6. Human entries with polymorphisms or disease mutations
    List of human entries with polymorphisms or disease mutations
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