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UniProtKB - Q9BYX4 (IFIH1_HUMAN)

Entry version 183 (10 Feb 2021)
Sequence version 3 (20 Mar 2007)
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Protein

Interferon-induced helicase C domain-containing protein 1

Gene

IFIH1

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 mRNA lacking 2'-O-methylation at their 5' cap and long-dsRNA (>1 kb in length). 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. Responsible for detecting the Picornaviridae family members such as encephalomyocarditis virus (EMCV) and mengo encephalomyocarditis virus (ENMG). Can also detect other viruses such as dengue virus (DENV), west Nile virus (WNV), and reovirus. Also involved in antiviral signaling in response to viruses containing a dsDNA genome, such as vaccinia virus. Plays an important role in amplifying innate immune signaling through recognition of RNA metabolites that are produced during virus infection by ribonuclease L (RNase L). May play an important role in enhancing natural killer cell function and may be involved in growth inhibition and apoptosis in several tumor cell lines.6 Publications

Miscellaneous

In HIV-1 infected HeLa-CD4 cells, overexpression of IFIH1 results in a great increase in the level of secreted viral p24 protein.

<p>This subsection of the <a href="http://www.uniprot.org/help/function%5Fsection">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 <a href="http://www.uniprot.org/help/function%5Fsection">Function</a> 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 bindingi907ZincPROSITE-ProRule annotation1
Metal bindingi910ZincPROSITE-ProRule annotation1
Metal bindingi962ZincPROSITE-ProRule annotation1
Metal bindingi964ZincPROSITE-ProRule annotation1

<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

Complete GO annotation on QuickGO ...

GO - Biological processi

Complete GO annotation on QuickGO ...

<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

Pathway Commons web resource for biological pathway data

More...PathwayCommonsi		Q9BYX4

Reactome - a knowledgebase of biological pathways and processes

More...Reactomei		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-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

More...SIGNORi		Q9BYX4

<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%5Fand%5Ftaxonomy%5Fsection">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:
Interferon-induced helicase C domain-containing protein 1 (EC:3.6.4.13)
Alternative name(s):
Clinically amyopathic dermatomyositis autoantigen 140 kDa
Short name:
CADM-140 autoantigen
Helicase with 2 CARD domains
Short name:
Helicard
Interferon-induced with helicase C domain protein 1
Melanoma differentiation-associated protein 5
Short name:
MDA-5
Murabutide down-regulated protein
RIG-I-like receptor 2
Short name:
RLR-2
RNA helicase-DEAD box protein 116
<p>This subsection of the <a href="http://www.uniprot.org/help/names%5Fand%5Ftaxonomy%5Fsection">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:IFIH1
Synonyms:MDA5, RH116
<p>This subsection of the <a href="http://www.uniprot.org/help/names%5Fand%5Ftaxonomy%5Fsection">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%5Fand%5Ftaxonomy%5Fsection">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%5Fand%5Ftaxonomy%5Fsection">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 lineageiEukaryota › Metazoa › Chordata › Craniata › Vertebrata › Euteleostomi › Mammalia › Eutheria › Euarchontoglires › Primates › Haplorrhini › Catarrhini › Hominidae › Homo
<p>This subsection of the <a href="http://www.uniprot.org/help/names%5Fand%5Ftaxonomy%5Fsection">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%5Fmanual">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 2

Organism-specific databases

Human Gene Nomenclature Database

More...HGNCi		HGNC:18873, IFIH1

Online Mendelian Inheritance in Man (OMIM)

More...MIMi		606951, gene

neXtProt; the human protein knowledge platform

More...neXtProti		NX_Q9BYX4

Eukaryotic Pathogen, Vector and Host Database Resources

More...VEuPathDBi		HostDB:ENSG00000115267.5

<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 & Seán O’Donoghue; Source: COMPARTMENTS

Keywords - Cellular componenti

Cytoplasm, Nucleus

<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

Diabetes mellitus, insulin-dependent, 19 (IDDM19)1 Publication
Disease susceptibility may be associated with variants affecting the gene represented in this entry.
Disease descriptionA multifactorial disorder of glucose homeostasis that is characterized by susceptibility to ketoacidosis in the absence of insulin therapy. Clinical features are polydipsia, polyphagia and polyuria which result from hyperglycemia-induced osmotic diuresis and secondary thirst. These derangements result in long-term complications that affect the eyes, kidneys, nerves, and blood vessels.
Related information in OMIM
IFIH1 is the CADM-140 autoantigen, involved in clinically amyopathic dermatomyositis (CADM). This is a chronic inflammatory disorder that shows typical skin manifestations of dermatomyositis but has no or little evidence of clinical myositis. Anti-CADM-140 antibodies appear to be specific to dermatomyositis, especially CADM. Patients with anti-CADM-140 antibodies frequently develop life-threatening acute progressive interstitial lung disease (ILD).2 Publications
Aicardi-Goutieres syndrome 7 (AGS7)2 Publications
The disease is caused by variants affecting the gene represented in this entry.
Disease descriptionA form of Aicardi-Goutieres syndrome, a genetically heterogeneous disease characterized by cerebral atrophy, leukoencephalopathy, intracranial calcifications, chronic cerebrospinal fluid (CSF) lymphocytosis, increased CSF alpha-interferon, and negative serologic investigations for common prenatal infection. Clinical features as thrombocytopenia, hepatosplenomegaly and elevated hepatic transaminases along with intermittent fever may erroneously suggest an infective process. Severe neurological dysfunctions manifest in infancy as progressive microcephaly, spasticity, dystonic posturing and profound psychomotor retardation. Death often occurs in early childhood.
Related information in OMIM
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_071375337R → G in AGS7; enhances the interferon signaling pathway activation; enhances the stability of filament formation; enhances dsRNA binding activity; no loss of ATP hydrolysis. 1 PublicationCorresponds to variant dbSNP:rs587777447EnsemblClinVar.1
Natural variantiVAR_071376372L → F in AGS7; enhances IFNB1 promoter activation; loss of ligand-induced responsiveness. 1 PublicationCorresponds to variant dbSNP:rs587777576EnsemblClinVar.1
Natural variantiVAR_071377393D → V in AGS7; enhances the interferon signaling pathway activation; enhances the stability of filament formation; enhances dsRNA binding activity; no loss of ATP hydrolysis. 1 PublicationCorresponds to variant dbSNP:rs587777449EnsemblClinVar.1
Natural variantiVAR_071378452A → T in AGS7; enhances IFNB1 promoter activation; loss of ligand-induced responsiveness. 1 PublicationCorresponds to variant dbSNP:rs587777575EnsemblClinVar.1
Natural variantiVAR_071379495G → R in AGS7; enhances the interferon signaling pathway activation; enhances the stability of filament formation; enhances dsRNA binding activity; no loss of ATP hydrolysis. 1 PublicationCorresponds to variant dbSNP:rs672601336EnsemblClinVar.1
Natural variantiVAR_071380720R → Q in AGS7; enhances the interferon signaling pathway activation; enhances the stability of filament formation; enhances dsRNA binding activity; no loss of ATP hydrolysis. 1 PublicationCorresponds to variant dbSNP:rs587777445EnsemblClinVar.1
Natural variantiVAR_071381779R → C in AGS7; enhances the interferon signaling pathway activation; enhances the stability of filament formation; enhances dsRNA binding activity; no loss of ATP hydrolysis. 1 PublicationCorresponds to variant dbSNP:rs587777448EnsemblClinVar.1
Natural variantiVAR_071382779R → H in AGS7; enhances the interferon signaling pathway activation; enhances the stability of filament formation; enhances dsRNA binding activity; enhances IFNB1 promoter activation; no loss of ATP hydrolysis. 2 PublicationsCorresponds to variant dbSNP:rs587777446EnsemblClinVar.1
Singleton-Merten syndrome 1 (SGMRT1)1 Publication
The disease is caused by variants affecting the gene represented in this entry.
Disease descriptionAn autosomal dominant disorder with variable expression. Core features are marked aortic calcification, dental anomalies, osteopenia, acro-osteolysis, and to a lesser extent glaucoma, psoriasis, muscle weakness, and joint laxity. Dental anomalies include delayed eruption and immature root formation of anterior permanent teeth, early loss of permanent teeth due to short roots, acute root resorption, high caries, and aggressive alveolar bone loss. Additional clinical manifestations include particular facial characteristics and abnormal joint and muscle ligaments.
Related information in OMIM
Feature keyPosition(s)DescriptionActionsGraphical viewLength
Natural variantiVAR_073666822R → Q in SGMRT1; gain-of-function mutation resulting in enhanced INFB1 induction. 1 PublicationCorresponds to variant dbSNP:rs376048533EnsemblClinVar.1

Mutagenesis

Feature keyPosition(s)DescriptionActionsGraphical viewLength
<p>This subsection of the <a href="http://www.uniprot.org/manual/pathology%5Fand%5Fbiotech%5Fsection">'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>Mutagenesisi251D → A: No cleavage and no acceleration of DNA degradation. 1 Publication1
Mutagenesisi444E → A: No acceleration of DNA degradation, no binding to ATP, and no helicase activity. 1 Publication1
Mutagenesisi828S → A: Promotes multimerization after polyI:C stimulation; greatly enhances signaling. 1 Publication1
Mutagenesisi828S → D: Inhibits multimerization after polyI:C stimulation. 1 Publication1
Mutagenesisi829T → A: Moderately increases signaling. 1 Publication1

Keywords - Diseasei

Aicardi-Goutieres syndrome, Diabetes mellitus, Disease variant

Organism-specific databases

DisGeNET

More...DisGeNETi		64135

GeneReviews a resource of expert-authored, peer-reviewed disease descriptions.

More...GeneReviewsi		IFIH1

MalaCards human disease database

More...MalaCardsi		IFIH1
MIMi182250, phenotype
610155, phenotype
615846, phenotype

Open Targets

More...OpenTargetsi		ENSG00000115267

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

More...Orphaneti		51, Aicardi-Goutieres syndrome
85191, Singleton-Merten dysplasia

The Pharmacogenetics and Pharmacogenomics Knowledge Base

More...PharmGKBi		PA134889215

Miscellaneous databases

Pharos NIH Druggable Genome Knowledgebase

More...Pharosi		Q9BYX4, Tbio

Genetic variation databases

BioMuta curated single-nucleotide variation and disease association database

More...BioMutai		IFIH1

Domain mapping of disease mutations (DMDM)

More...DMDMi		134047802

<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 or proteolytic cleavage.<p><a href='/help/chain' target='_top'>More...</a></p>ChainiPRO_00001020121 – 1025Interferon-induced helicase C domain-containing protein 1Add BLAST1025

Amino acid modifications

Feature keyPosition(s)DescriptionActionsGraphical viewLength
<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 residuei289PhosphoserineBy similarity1
Modified residuei291PhosphoserineBy similarity1
Modified residuei301PhosphoserineBy similarity1
Modified residuei645PhosphoserineBy similarity1
Modified residuei828Phosphoserine; by RIOK31 Publication1

<p>This subsection of the <a href="http://www.uniprot.org/help/ptm%5Fprocessing%5Fsection">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

Sumoylated. Sumoylation positively regulates its role in type I interferon induction and is enhanced by PIAS2-beta.1 Publication
Ubiquitinated by RNF125, leading to its degradation by the proteasome (PubMed:17460044). USP17/UPS17L2-dependent deubiquitination positively regulates the receptor (PubMed:20368735). Ubiquitinated by TRIM25 via 'Lys-63'-linked ubiquitination, promoting activation of IFIH1/MDA5 (PubMed:30193849). Ubiquitinated by TRIM40 via 'Lys-48'-linked ubiquitination; leading to proteasomal degradation (PubMed:29117565).4 Publications
During apoptosis, processed into 3 cleavage products. The helicase-containing fragment, once liberated from the CARD domains, translocate from the cytoplasm to the nucleus. The processed protein significantly sensitizes cells to DNA degradation.By similarity
(Microbial infection) Cleaved and inactivated by the protease 2A of coxsackievirus B3, poliovirus and enterovirus 71 allowing the virus to disrupt the host type I interferon production.1 Publication

Sites

Feature keyPosition(s)DescriptionActionsGraphical viewLength
<p>This subsection describes interesting single amino acid sites on the sequence that are not defined in any other subsection. This subsection can be displayed in different sections ('Function', 'PTM / Processing', 'Pathology and Biotech') according to its content.<p><a href='/help/site' target='_top'>More...</a></p>Sitei208 – 209CleavageBy similarity2
Sitei216 – 217CleavageBy similarity2
Sitei251 – 252CleavageBy similarity2

Keywords - PTMi

Phosphoprotein, Ubl conjugation

Proteomic databases

Encyclopedia of Proteome Dynamics

More...EPDi		Q9BYX4

jPOST - Japan Proteome Standard Repository/Database

More...jPOSTi		Q9BYX4

MassIVE - Mass Spectrometry Interactive Virtual Environment

More...MassIVEi		Q9BYX4

MaxQB - The MaxQuant DataBase

More...MaxQBi		Q9BYX4

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

More...PaxDbi		Q9BYX4

PeptideAtlas

More...PeptideAtlasi		Q9BYX4

PRoteomics IDEntifications database

More...PRIDEi		Q9BYX4

ProteomicsDB: a multi-organism proteome resource

More...ProteomicsDBi		79740 [Q9BYX4-1]
79741 [Q9BYX4-2]

PTM databases

iPTMnet integrated resource for PTMs in systems biology context

More...iPTMneti		Q9BYX4

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

More...PhosphoSitePlusi		Q9BYX4

<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

Widely expressed, at a low level. Expression is detected at slightly highest levels in placenta, pancreas and spleen and at barely levels in detectable brain, testis and lung.3 Publications

<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 interferon (IFN) and TNF.1 Publication

Gene expression databases

Bgee dataBase for Gene Expression Evolution

More...Bgeei		ENSG00000115267, Expressed in parotid gland and 224 other tissues

ExpressionAtlas, Differential and Baseline Expression

More...ExpressionAtlasi		Q9BYX4, baseline and differential

Genevisible search portal to normalized and curated expression data from Genevestigator

More...Genevisiblei		Q9BYX4, HS

Organism-specific databases

Human Protein Atlas

More...HPAi		ENSG00000115267, Low tissue specificity

<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%5Fsection">'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%5Fsection">'Function'</a> section).<p><a href='/help/subunit_structure' target='_top'>More...</a></p>Subunit structurei

Monomer in the absence of ligands and homodimerizes in the presence of dsRNA ligands. Can assemble into helical or linear polymeric filaments on long dsRNA.

Interacts with MAVS/IPS1.

Interacts (via the CARD domains) with TKFC, the interaction is inhibited by viral infection (PubMed:17600090).

Interacts with PCBP2.

Interacts with NLRC5.

Interacts with PIAS2-beta.

Interacts with DDX60.

Interacts with ANKRD17.

Interacts with IKBKE (PubMed:17600090).

Interacts with ATG5 and ATG12, either as ATG5 and ATG12 monomers or as ATG12-ATG5 conjugates (PubMed:17709747).

Interacts with ZCCHC3; leading to activate IFIH1/MDA5 (PubMed:30193849).

Interacts with RNF123 (PubMed:27312109).

Interacts with DDX3X (PubMed:20127681).

16 Publications

(Microbial infection) Interacts with V protein of paramyxoviruses; these interactions prevent IFN-beta induction, and subsquent establishment of an antiviral state.

1 Publication

(Microbial infection) Interacts with herpes simplex virus 1 protein US11; this interaction prevents the interaction of MAVS/IPS1 to IFIH1.

1 Publication

(Microbial infection) Interacts with Encephalomyocarditis virus protein 2C; this interaction inhibits the induction of the IFN-beta signal pathway.

1 Publication

(Microbial infection) Interacts with protease 3C of coxsackievirus A16; this interaction inhibits IFIH1 thereby attenuating type-I IFN production.

1 Publication

<p>This subsection of the '<a href="http://www.uniprot.org/help/interaction%5Fsection">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="https://www.ebi.ac.uk/intact/">IntAct database</a>. It is updated at every <a href="http://www.uniprot.org/help/synchronization">UniProt release</a>.<p><a href='/help/binary_interactions' target='_top'>More...</a></p>Binary interactionsi

Hide details

GO - Molecular functioni

Complete GO annotation on QuickGO ...

Protein-protein interaction databases

The Biological General Repository for Interaction Datasets (BioGRID)

More...BioGRIDi		122082, 28 interactors

Database of interacting proteins

More...DIPi		DIP-42607N

Protein interaction database and analysis system

More...IntActi		Q9BYX4, 47 interactors

STRING: functional protein association networks

More...STRINGi		9606.ENSP00000263642

Miscellaneous databases

RNAct, Protein-RNA interaction predictions for model organisms.

More...RNActi		Q9BYX4, protein

<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

11025
Legend: HelixTurnBeta strandPDB Structure known for this area
Show more details

3D structure databases

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

More...SMRi		Q9BYX4

Database of comparative protein structure models

More...ModBasei		Search...

Protein Data Bank in Europe - Knowledge Base

More...PDBe-KBi		Search...

Miscellaneous databases

Relative evolutionary importance of amino acids within a protein sequence

More...EvolutionaryTracei		Q9BYX4

<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%5Fand%5Fdomains%5Fsection">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>Domaini7 – 97CARD 1Add BLAST91
Domaini110 – 190CARD 2Add BLAST81
Domaini316 – 509Helicase ATP-bindingPROSITE-ProRule annotationAdd BLAST194
Domaini700 – 882Helicase C-terminalPROSITE-ProRule annotationAdd BLAST183
Domaini893 – 1020RLR CTRPROSITE-ProRule annotationAdd BLAST128

<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

Ensembl GeneTree

More...GeneTreei		ENSGT00940000153173

The HOGENOM Database of Homologous Genes from Fully Sequenced Organisms

More...HOGENOMi		CLU_006888_0_0_1

InParanoid: Eukaryotic Ortholog Groups

More...InParanoidi		Q9BYX4

Identification of Orthologs from Complete Genome Data

More...OMAi		CCLFSDE

Database of Orthologous Groups

More...OrthoDBi		1337630at2759

Database for complete collections of gene phylogenies

More...PhylomeDBi		Q9BYX4

TreeFam database of animal gene trees

More...TreeFami		TF330258

Family and domain databases

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
IPR006935, Helicase/UvrB_N
IPR014001, Helicase_ATP-bd
IPR001650, Helicase_C
IPR027417, P-loop_NTPase
IPR041204, RIG-I_C
IPR038557, RLR_C_sf
IPR021673, RLR_CTR

Pfam protein domain database

More...Pfami		View protein in Pfam
PF16739, CARD_2, 2 hits
PF00271, Helicase_C, 1 hit
PF04851, ResIII, 1 hit
PF18119, RIG-I_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%5Flength">length</a> and <a href="http://www.uniprot.org/help/sequences">molecular weight</a>. The information is filed in different subsections. The current subsections and their content are listed below:<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%5Fsection">Sequence</a> section indicates if the <a href="http://www.uniprot.org/help/canonical%5Fand%5Fisoforms">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. This section is only present in reviewed entries, i.e. in UniProtKB/Swiss-Prot.<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: Q9BYX4-1) [UniParc]FASTAAdd to basket

This isoform has been chosen as the <div> <p><b>What is the canonical sequence?</b><p><a href='/help/canonical_and_isoforms' target='_top'>More...</a></p>canonicali 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
MSNGYSTDEN FRYLISCFRA RVKMYIQVEP VLDYLTFLPA EVKEQIQRTV 
        60         70         80         90        100
ATSGNMQAVE LLLSTLEKGV WHLGWTREFV EALRRTGSPL AARYMNPELT 
       110        120        130        140        150
DLPSPSFENA HDEYLQLLNL LQPTLVDKLL VRDVLDKCME EELLTIEDRN 
       160        170        180        190        200
RIAAAENNGN ESGVRELLKR IVQKENWFSA FLNVLRQTGN NELVQELTGS 
       210        220        230        240        250
DCSESNAEIE NLSQVDGPQV EEQLLSTTVQ PNLEKEVWGM ENNSSESSFA 
       260        270        280        290        300
DSSVVSESDT SLAEGSVSCL DESLGHNSNM GSDSGTMGSD SDEENVAARA 
       310        320        330        340        350
SPEPELQLRP YQMEVAQPAL EGKNIIICLP TGSGKTRVAV YIAKDHLDKK 
       360        370        380        390        400
KKASEPGKVI VLVNKVLLVE QLFRKEFQPF LKKWYRVIGL SGDTQLKISF 
       410        420        430        440        450
PEVVKSCDII ISTAQILENS LLNLENGEDA GVQLSDFSLI IIDECHHTNK 
       460        470        480        490        500
EAVYNNIMRH YLMQKLKNNR LKKENKPVIP LPQILGLTAS PGVGGATKQA 
       510        520        530        540        550
KAEEHILKLC ANLDAFTIKT VKENLDQLKN QIQEPCKKFA IADATREDPF 
       560        570        580        590        600
KEKLLEIMTR IQTYCQMSPM SDFGTQPYEQ WAIQMEKKAA KEGNRKERVC 
       610        620        630        640        650
AEHLRKYNEA LQINDTIRMI DAYTHLETFY NEEKDKKFAV IEDDSDEGGD 
       660        670        680        690        700
DEYCDGDEDE DDLKKPLKLD ETDRFLMTLF FENNKMLKRL AENPEYENEK 
       710        720        730        740        750
LTKLRNTIME QYTRTEESAR GIIFTKTRQS AYALSQWITE NEKFAEVGVK 
       760        770        780        790        800
AHHLIGAGHS SEFKPMTQNE QKEVISKFRT GKINLLIATT VAEEGLDIKE 
       810        820        830        840        850
CNIVIRYGLV TNEIAMVQAR GRARADESTY VLVAHSGSGV IEHETVNDFR 
       860        870        880        890        900
EKMMYKAIHC VQNMKPEEYA HKILELQMQS IMEKKMKTKR NIAKHYKNNP 
       910        920        930        940        950
SLITFLCKNC SVLACSGEDI HVIEKMHHVN MTPEFKELYI VRENKALQKK 
       960        970        980        990       1000
CADYQINGEI ICKCGQAWGT MMVHKGLDLP CLKIRNFVVV FKNNSTKKQY 
      1010       1020 
KKWVELPITF PNLDYSECCL FSDED
Length:1,025
Mass (Da):116,689
Last modified:March 20, 2007 - v3
<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:i789CFB4824B92DC9
GO
Isoform 2 (identifier: Q9BYX4-2) [UniParc]FASTAAdd to basket

The sequence of this isoform differs from the canonical sequence as follows:
     208-221: EIENLSQVDGPQVE → GICNFTEEDSSNSA
     222-1025: Missing.

Show »
Length:221
Mass (Da):25,129
Checksum:i3C7139ECAC564BB5
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
A0A3B3IRK8A0A3B3IRK8_HUMAN
RNA helicase
IFIH1
986Annotation score:

Annotation score:3 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>

<p>This subsection of the 'Sequence' section reports difference(s) between the protein sequence shown in the UniProtKB entry and other available protein sequences derived from the same gene.<p><a href='/help/sequence_caution' target='_top'>More...</a></p>Sequence cautioni

The sequence AAH78180 differs from that shown. Contaminating sequence. Potential poly-A sequence.Curated
The sequence BAB71141 differs from that shown. Reason: Erroneous initiation. Truncated N-terminus.Curated

Experimental Info

Feature keyPosition(s)DescriptionActionsGraphical viewLength
<p>This subsection of the 'Sequence' section reports difference(s) between the canonical sequence (displayed by default in the entry) and the different sequence submissions merged in the entry. These various submissions may originate from different sequencing projects, different types of experiments, or different biological samples. Sequence conflicts are usually of unknown origin.<p><a href='/help/conflict' target='_top'>More...</a></p>Sequence conflicti439L → F in AAG54076 (PubMed:14645903).Curated1
Sequence conflicti475N → H in BAB71141 (PubMed:14702039).Curated1
Sequence conflicti592E → K in AAG34368 (PubMed:11805321).Curated1
Sequence conflicti598R → S in AAG54076 (PubMed:14645903).Curated1
Sequence conflicti609E → K in AAG54076 (PubMed:14645903).Curated1
Sequence conflicti782K → R in BAB71141 (PubMed:14702039).Curated1

Natural variant

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Natural variantiVAR_071375337R → G in AGS7; enhances the interferon signaling pathway activation; enhances the stability of filament formation; enhances dsRNA binding activity; no loss of ATP hydrolysis. 1 PublicationCorresponds to variant dbSNP:rs587777447EnsemblClinVar.1
Natural variantiVAR_071376372L → F in AGS7; enhances IFNB1 promoter activation; loss of ligand-induced responsiveness. 1 PublicationCorresponds to variant dbSNP:rs587777576EnsemblClinVar.1
Natural variantiVAR_071377393D → V in AGS7; enhances the interferon signaling pathway activation; enhances the stability of filament formation; enhances dsRNA binding activity; no loss of ATP hydrolysis. 1 PublicationCorresponds to variant dbSNP:rs587777449EnsemblClinVar.1
Natural variantiVAR_071378452A → T in AGS7; enhances IFNB1 promoter activation; loss of ligand-induced responsiveness. 1 PublicationCorresponds to variant dbSNP:rs587777575EnsemblClinVar.1
Natural variantiVAR_031226460H → R. Corresponds to variant dbSNP:rs10930046Ensembl.1
Natural variantiVAR_071379495G → R in AGS7; enhances the interferon signaling pathway activation; enhances the stability of filament formation; enhances dsRNA binding activity; no loss of ATP hydrolysis. 1 PublicationCorresponds to variant dbSNP:rs672601336EnsemblClinVar.1
Natural variantiVAR_071380720R → Q in AGS7; enhances the interferon signaling pathway activation; enhances the stability of filament formation; enhances dsRNA binding activity; no loss of ATP hydrolysis. 1 PublicationCorresponds to variant dbSNP:rs587777445EnsemblClinVar.1
Natural variantiVAR_071381779R → C in AGS7; enhances the interferon signaling pathway activation; enhances the stability of filament formation; enhances dsRNA binding activity; no loss of ATP hydrolysis. 1 PublicationCorresponds to variant dbSNP:rs587777448EnsemblClinVar.1
Natural variantiVAR_071382779R → H in AGS7; enhances the interferon signaling pathway activation; enhances the stability of filament formation; enhances dsRNA binding activity; enhances IFNB1 promoter activation; no loss of ATP hydrolysis. 2 PublicationsCorresponds to variant dbSNP:rs587777446EnsemblClinVar.1
Natural variantiVAR_073666822R → Q in SGMRT1; gain-of-function mutation resulting in enhanced INFB1 induction. 1 PublicationCorresponds to variant dbSNP:rs376048533EnsemblClinVar.1
Natural variantiVAR_021594843H → R3 PublicationsCorresponds to variant dbSNP:rs3747517EnsemblClinVar.1
Natural variantiVAR_021595946A → T Associated with susceptibility to IDDM19. 3 PublicationsCorresponds to variant dbSNP:rs1990760EnsemblClinVar.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.<p><a href='/help/var_seq' target='_top'>More...</a></p>Alternative sequenceiVSP_013337208 – 221EIENL…GPQVE → GICNFTEEDSSNSA in isoform 2. 1 PublicationAdd BLAST14
Alternative sequenceiVSP_013338222 – 1025Missing in isoform 2. 1 PublicationAdd BLAST804

Sequence databases

Select the link destinations:

EMBL nucleotide sequence database

More...EMBLi

GenBank nucleotide sequence database

More...GenBanki

DNA Data Bank of Japan; a nucleotide sequence database

More...DDBJi
Links Updated
AF095844 mRNA Translation: AAG34368.1
AY017378 mRNA Translation: AAG54076.1
BC046208 mRNA Translation: AAH46208.1
BC078180 mRNA Translation: AAH78180.1 Sequence problems.
BC111750 mRNA Translation: AAI11751.1
AK056293 mRNA Translation: BAB71141.1 Different initiation.

The Consensus CDS (CCDS) project

More...CCDSi		CCDS2217.1 [Q9BYX4-1]

NCBI Reference Sequences

More...RefSeqi		NP_071451.2, NM_022168.3 [Q9BYX4-1]

Genome annotation databases

Ensembl eukaryotic genome annotation project

More...Ensembli		ENST00000421365; ENSP00000408450; ENSG00000115267 [Q9BYX4-2]
ENST00000649979; ENSP00000497271; ENSG00000115267 [Q9BYX4-1]

Database of genes from NCBI RefSeq genomes

More...GeneIDi		64135

KEGG: Kyoto Encyclopedia of Genes and Genomes

More...KEGGi		hsa:64135

UCSC genome browser

More...UCSCi		uc002uce.5, human [Q9BYX4-1]

Keywords - Coding sequence diversityi

Alternative splicing

<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
AF095844 mRNA Translation: AAG34368.1
AY017378 mRNA Translation: AAG54076.1
BC046208 mRNA Translation: AAH46208.1
BC078180 mRNA Translation: AAH78180.1 Sequence problems.
BC111750 mRNA Translation: AAI11751.1
AK056293 mRNA Translation: BAB71141.1 Different initiation.
CCDSiCCDS2217.1 [Q9BYX4-1]
RefSeqiNP_071451.2, NM_022168.3 [Q9BYX4-1]

3D structure databases

Select the link destinations:

Protein Data Bank Europe

More...PDBei

Protein Data Bank RCSB

More...RCSB PDBi

Protein Data Bank Japan

More...PDBji
Links Updated
PDB entryMethodResolution (Å)ChainPositionsPDBsum
2RQBNMR-A896-1025[»]
3B6EX-ray1.60A277-490[»]
3GA3X-ray1.45A893-1017[»]
4GL2X-ray3.56A/B306-1017[»]
SMRiQ9BYX4
ModBaseiSearch...
PDBe-KBiSearch...

Protein-protein interaction databases

BioGRIDi122082, 28 interactors
DIPiDIP-42607N
IntActiQ9BYX4, 47 interactors
STRINGi9606.ENSP00000263642

PTM databases

iPTMnetiQ9BYX4
PhosphoSitePlusiQ9BYX4

Genetic variation databases

BioMutaiIFIH1
DMDMi134047802

Proteomic databases

EPDiQ9BYX4
jPOSTiQ9BYX4
MassIVEiQ9BYX4
MaxQBiQ9BYX4
PaxDbiQ9BYX4
PeptideAtlasiQ9BYX4
PRIDEiQ9BYX4
ProteomicsDBi79740 [Q9BYX4-1]
79741 [Q9BYX4-2]

Protocols and materials databases

Antibodypedia a portal for validated antibodies

More...Antibodypediai		805, 480 antibodies

Genome annotation databases

EnsembliENST00000421365; ENSP00000408450; ENSG00000115267 [Q9BYX4-2]
ENST00000649979; ENSP00000497271; ENSG00000115267 [Q9BYX4-1]
GeneIDi64135
KEGGihsa:64135
UCSCiuc002uce.5, human [Q9BYX4-1]

Organism-specific databases

Comparative Toxicogenomics Database

More...CTDi		64135
DisGeNETi64135

GeneCards: human genes, protein and diseases

More...GeneCardsi		IFIH1
GeneReviewsiIFIH1
HGNCiHGNC:18873, IFIH1
HPAiENSG00000115267, Low tissue specificity
MalaCardsiIFIH1
MIMi182250, phenotype
606951, gene
610155, phenotype
615846, phenotype
neXtProtiNX_Q9BYX4
OpenTargetsiENSG00000115267
Orphaneti51, Aicardi-Goutieres syndrome
85191, Singleton-Merten dysplasia
PharmGKBiPA134889215
VEuPathDBiHostDB:ENSG00000115267.5

GenAtlas: human gene database

More...GenAtlasi		Search...

Phylogenomic databases

eggNOGiKOG0354, Eukaryota
GeneTreeiENSGT00940000153173
HOGENOMiCLU_006888_0_0_1
InParanoidiQ9BYX4
OMAiCCLFSDE
OrthoDBi1337630at2759
PhylomeDBiQ9BYX4
TreeFamiTF330258

Enzyme and pathway databases

PathwayCommonsiQ9BYX4
ReactomeiR-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-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
SIGNORiQ9BYX4

Miscellaneous databases

BioGRID ORCS database of CRISPR phenotype screens

More...BioGRID-ORCSi		64135, 3 hits in 877 CRISPR screens

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

More...ChiTaRSi		IFIH1, human
EvolutionaryTraceiQ9BYX4

The Gene Wiki collection of pages on human genes and proteins

More...GeneWikii		MDA5

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

More...GenomeRNAii		64135
PharosiQ9BYX4, Tbio

Protein Ontology

More...PROi		PR:Q9BYX4
RNActiQ9BYX4, protein

The Stanford Online Universal Resource for Clones and ESTs

More...SOURCEi		Search...

Gene expression databases

BgeeiENSG00000115267, Expressed in parotid gland and 224 other tissues
ExpressionAtlasiQ9BYX4, baseline and differential
GenevisibleiQ9BYX4, HS

Family and domain databases

Gene3Di2.170.150.30, 1 hit
InterProiView protein in InterPro
IPR031964, CARD_dom
IPR006935, Helicase/UvrB_N
IPR014001, Helicase_ATP-bd
IPR001650, Helicase_C
IPR027417, P-loop_NTPase
IPR041204, RIG-I_C
IPR038557, RLR_C_sf
IPR021673, RLR_CTR
PfamiView protein in Pfam
PF16739, CARD_2, 2 hits
PF00271, Helicase_C, 1 hit
PF04851, ResIII, 1 hit
PF18119, RIG-I_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...

MobiDB: a database of protein disorder and mobility annotations

More...MobiDBi		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 nameiIFIH1_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: Q9BYX4
Secondary accession number(s): Q2NKL6
, Q6DC96, Q86X56, Q96MX8, Q9H3G6
<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%5Fand%5Fisoforms">canonical sequence</a> are also displayed.<p><a href='/help/entry_history' target='_top'>More...</a></p>Entry historyiIntegrated into UniProtKB/Swiss-Prot: April 12, 2005
Last sequence update: March 20, 2007
Last modified: February 10, 2021
This is version 183 of the entry and version 3 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, Reference proteome

Documents

  1. Human chromosome 2
    Human chromosome 2: entries, gene names and cross-references to MIM
  2. Human entries with genetic variants
    List of human entries with genetic variants
  3. Human variants curated from literature reports
    Index of human variants curated from literature reports
  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. SIMILARITY comments
    Index of protein domains and families
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