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Entry version 224 (16 Oct 2019)
Sequence version 3 (23 Jan 2007)
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Protein

ATP-dependent RNA helicase DDX3X

Gene

DDX3X

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

Multifunctional ATP-dependent RNA helicase. The ATPase activity can be stimulated by various ribo- and deoxynucleic acids indicative for a relaxed substrate specificity. In vitro can unwind partially double-stranded DNA with a preference for 5'-single-stranded DNA overhangs. Is involved in several steps of gene expression, such as transcription, mRNA maturation, mRNA export and translation. However, the exact mechanisms are not known and some functions may be specific for a subset of mRNAs. Involved in transcriptional regulation. Can enhance transcription from the CDKN1A/WAF1 promoter in a SP1-dependent manner. Found associated with the E-cadherin promoter and can down-regulate transcription from the promoter. Involved in regulation of translation initiation. Proposed to be involved in positive regulation of translation such as of cyclin E1/CCNE1 mRNA and specifically of mRNAs containing complex secondary structures in their 5'UTRs; these functions seem to require RNA helicase activity. Specifically promotes translation of a subset of viral and cellular mRNAs carrying a 5'proximal stem-loop structure in their 5'UTRs and cooperates with the eIF4F complex. Proposed to act prior to 43S ribosomal scanning and to locally destabilize these RNA structures to allow recognition of the mRNA cap or loading onto the 40S subunit. After association with 40S ribosomal subunits seems to be involved in the functional assembly of 80S ribosomes; the function seems to cover translation of mRNAs with structured and non-structured 5'UTRs and is independent of RNA helicase activity. Also proposed to inhibit cap-dependent translation by competetive interaction with EIF4E which can block the EIF4E:EIF4G complex formation. Proposed to be involved in stress response and stress granule assembly; the function is independent of RNA helicase activity and seems to involve association with EIF4E. May be involved in nuclear export of specific mRNAs but not in bulk mRNA export via interactions with XPO1 and NXF1. Also associates with polyadenylated mRNAs independently of NXF1. Associates with spliced mRNAs in an exon junction complex (EJC)-dependent manner and seems not to be directly involved in splicing. May be involved in nuclear mRNA export by association with DDX5 and regulating its nuclear location. Involved in innate immune signaling promoting the production of type I interferon (IFN-alpha and IFN-beta); proposed to act as viral RNA sensor, signaling intermediate and transcriptional coactivator. Involved in TBK1 and IKBKE-dependent IRF3 activation leading to IFNB induction, plays a role of scaffolding adapter that links IKBKE and IRF3 and coordinates their activation. Also found associated with IFNB promoters; the function is independent of IRF3. Can bind to viral RNAs and via association with MAVS/IPS1 and DDX58/RIG-I is thought to induce signaling in early stages of infection. Involved in regulation of apoptosis. May be required for activation of the intrinsic but inhibit activation of the extrinsic apoptotic pathway. Acts as an antiapoptotic protein through association with GSK3A/B and BIRC2 in an apoptosis antagonizing signaling complex; activation of death receptors promotes caspase-dependent cleavage of BIRC2 and DDX3X and relieves the inhibition. May be involved in mitotic chromosome segregation. Is an allosteric activator of CSNK1E, it stimulates CSNK1E-mediated phosphorylation of DVL2 and is involved in the positive regulation of canonical Wnt signaling (PubMed:23413191).22 Publications
(Microbial infection) Appears to be a prime target for viral manipulations. Hepatitis B virus (HBV) polymerase and possibly vaccinia virus (VACV) protein K7 inhibit IFNB induction probably by dissociating DDX3X from TBK1 or IKBKE. Is involved in hepatitis C virus (HCV) replication; the function may involve the association with HCV core protein. HCV core protein inhibits the IPS1-dependent function in viral RNA sensing and may switch the function from a INFB inducing to a HCV replication mode. Involved in HIV-1 replication. Acts as a cofactor for XPO1-mediated nuclear export of incompletely spliced HIV-1 Rev RNAs.3 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

Regions

Feature keyPosition(s)DescriptionActionsGraphical viewLength
<p>This subsection of the <a href="http://www.uniprot.org/help/function_section">Function</a> 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 bindingi200 – 207ATP8
Nucleotide bindingi224 – 231ATP8

<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

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 functionDNA-binding, Helicase, Hydrolase, RNA-binding
Biological processApoptosis, Chromosome partition, Host-virus interaction, Immunity, Innate immunity, Ribosome biogenesis, Transcription, Transcription regulation, Translation regulation
LigandATP-binding, Nucleotide-binding

Enzyme and pathway databases

BRENDA Comprehensive Enzyme Information System

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BRENDAi
3.6.4.13 2681

Reactome - a knowledgebase of biological pathways and processes

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Reactomei
R-HSA-6798695 Neutrophil degranulation

SIGNOR Signaling Network Open Resource

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SIGNORi
O00571

Protein family/group databases

Transport Classification Database

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TCDBi
1.I.1.1.3 the eukaryotic nuclear pore complex (e-npc) family

<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:
ATP-dependent RNA helicase DDX3X (EC:3.6.4.13)
Alternative name(s):
DEAD box protein 3, X-chromosomal
DEAD box, X isoform
Helicase-like protein 2
Short name:
HLP2
<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:DDX3X
Synonyms:DBX, DDX3
<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 X

Organism-specific databases

Human Gene Nomenclature Database

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HGNCi
HGNC:2745 DDX3X

Online Mendelian Inheritance in Man (OMIM)

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MIMi
300160 gene

neXtProt; the human protein knowledge platform

More...
neXtProti
NX_O00571

<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, Membrane, Mitochondrion, Mitochondrion outer membrane, 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

Mental retardation, X-linked 102 (MRX102)1 Publication
The disease is caused by mutations affecting the gene represented in this entry.
Disease descriptionA form of mental retardation, a disorder characterized by significantly below average general intellectual functioning associated with impairments in adaptive behavior and manifested during the developmental period. Intellectual deficiency is the only primary symptom of non-syndromic X-linked mental retardation, while syndromic mental retardation presents with associated physical, neurological and/or psychiatric manifestations. MRX102 features include mild to severe intellectual disability, hypotonia, movement disorders, behavior problems, corpus callosum hypoplasia, and epilepsy. Additionally, patients manifest variable non-neurologic features such as joint hyperlaxity, skin pigmentary abnormalities, cleft lip and/or palate, hearing and visual impairment, and precocious puberty.
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_075731214I → T in MRX102; loss-of-function mutation affecting regulation of Wnt signaling. 1 Publication1
Natural variantiVAR_075732233A → V in MRX102. 1 PublicationCorresponds to variant dbSNP:rs796052223Ensembl.1
Natural variantiVAR_075733233Missing in MRX102. 1 Publication1
Natural variantiVAR_075734235L → P in MRX102. 1 PublicationCorresponds to variant dbSNP:rs796052224Ensembl.1
Natural variantiVAR_075735300V → F in MRX102. 1 Publication1
Natural variantiVAR_075736326R → H in MRX102; loss-of-function mutation affecting regulation of Wnt signaling. 1 PublicationCorresponds to variant dbSNP:rs797045025EnsemblClinVar.1
Natural variantiVAR_075737351R → Q in MRX102. 1 PublicationCorresponds to variant dbSNP:rs1057518707EnsemblClinVar.1
Natural variantiVAR_075738362R → C in MRX102. 1 PublicationCorresponds to variant dbSNP:rs797045026EnsemblClinVar.1
Natural variantiVAR_075739376R → C in MRX102; loss-of-function mutation affecting regulation of Wnt signaling. 1 PublicationCorresponds to variant dbSNP:rs796052231EnsemblClinVar.1
Natural variantiVAR_075740392L → P in MRX102. 1 PublicationCorresponds to variant dbSNP:rs796052232Ensembl.1
Natural variantiVAR_075741417Q → P in MRX102. 1 PublicationCorresponds to variant dbSNP:rs796052233Ensembl.1
Natural variantiVAR_075742475R → G in MRX102. 1 PublicationCorresponds to variant dbSNP:rs1064794574EnsemblClinVar.1
Natural variantiVAR_075743480R → S in MRX102. 1 Publication1
Natural variantiVAR_075744488R → H in MRX102. 1 PublicationCorresponds to variant dbSNP:rs796052235EnsemblClinVar.1
Natural variantiVAR_075745507I → T in MRX102; loss-of-function mutation affecting regulation of Wnt signaling. 1 PublicationCorresponds to variant dbSNP:rs797045024EnsemblClinVar.1
Natural variantiVAR_075746509N → I in MRX102. 1 Publication1
Natural variantiVAR_075747514I → T in MRX102. 1 PublicationCorresponds to variant dbSNP:rs796052226EnsemblClinVar.1
Natural variantiVAR_075748534R → H in MRX102; loss-of-function mutation affecting regulation of Wnt signaling. 1 Publication1
Natural variantiVAR_075749560Missing in MRX102. 1 Publication1
Natural variantiVAR_075750568P → L in MRX102. 1 PublicationCorresponds to variant dbSNP:rs1057519430EnsemblClinVar.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>Mutagenesisi38Y → A: Impairs interaction with EIF4E. No effect on translation of HIV-1 RNA; when associated with A-43. 2 Publications1
Mutagenesisi43L → A: Impairs interaction with EIF4E. Fails to induce stress granule assembly and to rescue cell viability after stress. No effect on translation of HIV-1 RNA; when associated with A-38. 2 Publications1
Mutagenesisi71S → A: Reduces total phosphorylation by 60%. No effect on interaction with IKBKE. 1 Publication1
Mutagenesisi82 – 83SS → AA: Reduces total phosphorylation by 50%. No effect on interaction with IKBKE. 1 Publication2
Mutagenesisi84 – 85FF → AA: Abolishes interaction with VACV protein K7, IRF3 activation and IFN-beta promoter induction. 1 Publication2
Mutagenesisi102S → A: Reduces total phosphorylation by 30%. Abolishes interaction with IRF3 and fails to enhance IFNB promoter induction. No effect on interaction with IKBKE. 1 Publication1
Mutagenesisi102S → D: Interacts with IRF3 and enhances IFNB promoter induction. 1 Publication1
Mutagenesisi152S → A: Reduces total phosphorylation by 60%. No effect on interaction with IKBKE. 1 Publication1
Mutagenesisi181S → A: Greatly impairs phosphorylation by TBK1 and fails to synergize with TBK1 in IFN-beta induction; when associated with A-183; A-240 and A-269. 1 Publication1
Mutagenesisi183S → A: Greatly impairs phosphorylation by TBK1 and fails to synergize with TBK1 in IFN-beta induction; when associated with A-181; A-240 and A-269. 1 Publication1
Mutagenesisi200Y → A: No effect on general translation; when associated with A-207; A-230; A-347 and A-348. 1 Publication1
Mutagenesisi207Q → A: Inhibits translation of HIV-1 RNA. No effect on general translation; when associated with A-200; A-230: A-347 and A-348. 2 Publications1
Mutagenesisi230K → A: No effect on general translation; when associated with A-200; A-207; A-347 and A-348. 3 Publications1
Mutagenesisi230K → E: Abolishes ATPase activity and RNA-unwinding activity. Inhibits translation of HIV-1 RNA. 3 Publications1
Mutagenesisi240S → A: Greatly impairs phosphorylation by TBK1 and fails to synergize with TBK1 in IFN-beta induction; when associated with A-181; A-183 and A-269. 1 Publication1
Mutagenesisi269S → A: Greatly impairs phosphorylation by TBK1 and fails to synergize with TBK1 in IFN-beta induction; when associated with A-181; A-183 and A-240. 1 Publication1
Mutagenesisi347D → A: No effect on general translation; when associated with A-200; A-207; A-230 and A-348. 1 Publication1
Mutagenesisi348E → A: No effect on general translation; when associated with A-200; A-207; A-230 and A-347. 2 Publications1
Mutagenesisi348E → Q: Inhibits translation of HIV-1 RNA. 2 Publications1
Mutagenesisi382S → L: Abolishes ATPase activity and RNA-unwinding activity. No effect on translation of HIV-1 RNA. 2 Publications1
Mutagenesisi429S → A: Impairs phosphorylation by TBK1 and fails to synergize with TBK1 in IFN-beta induction; when associated with A-438; A-442; A-456 and A-520. 1 Publication1
Mutagenesisi438T → A: Impairs phosphorylation by TBK1 and fails to synergize with TBK1 in IFN-beta induction; when associated with A-429; A-442; A-456 and A-520. 1 Publication1
Mutagenesisi442S → A: Impairs phosphorylation by TBK1 and fails to synergize with TBK1 in IFN-beta induction; when associated with A-429; A-438; A-456 and A-520. 1 Publication1
Mutagenesisi456S → A: Impairs phosphorylation by TBK1 and fails to synergize with TBK1 in IFN-beta induction; when associated with A-429; A-438; A-442 and A-520. 1 Publication1
Mutagenesisi520S → A: Impairs phosphorylation by TBK1 and fails to synergize with TBK1 in IFN-beta induction; when associated with A-429; A-438; A-442 and A-456. 1 Publication1

Keywords - Diseasei

Disease mutation, Mental retardation

Organism-specific databases

DisGeNET

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DisGeNETi
1654

MalaCards human disease database

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MalaCardsi
DDX3X
MIMi300958 phenotype

Open Targets

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OpenTargetsi
ENSG00000215301

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

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Orphaneti
99861 Precursor T-cell acute lymphoblastic leukemia
3338 Toriello-Carey syndrome
457260 X-linked intellectual disability-hypotonia-movement disorder syndrome

The Pharmacogenetics and Pharmacogenomics Knowledge Base

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PharmGKBi
PA27216

Miscellaneous databases

Pharos NIH Druggable Genome Knowledgebase

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Pharosi
O00571

Chemistry databases

ChEMBL database of bioactive drug-like small molecules

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ChEMBLi
CHEMBL5553

Polymorphism and mutation databases

BioMuta curated single-nucleotide variation and disease association database

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BioMutai
DDX3X

<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 <a href="http://www.uniprot.org/help/ptm_processing_section">PTM / Processing</a> section indicates that the initiator methionine is cleaved from the mature protein.<p><a href='/help/init_met' target='_top'>More...</a></p>Initiator methionineiRemovedCombined sources1 Publication
<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_00000550092 – 662ATP-dependent RNA helicase DDX3XAdd BLAST661

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 residuei2N-acetylserineCombined sources1 Publication1
Modified residuei55N6-acetyllysineBy similarity1
Modified residuei82PhosphoserineCombined sources1
Modified residuei86PhosphoserineCombined sources1
Modified residuei90PhosphoserineCombined sources1
Modified residuei101Omega-N-methylarginineBy similarity1
Modified residuei102Phosphoserine; by IKKE1 Publication1
Modified residuei104PhosphotyrosineBy similarity1
Modified residuei110Omega-N-methylarginineBy similarity1
Modified residuei118N6-acetyllysineCombined sources1
Modified residuei131PhosphoserineCombined sources1
Modified residuei183PhosphoserineCombined sources1
<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-linki215Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO2)Combined sources
Modified residuei456PhosphoserineBy similarity1
Modified residuei592Omega-N-methylarginineCombined sources1
Modified residuei594PhosphoserineCombined sources1
Modified residuei605PhosphoserineCombined sources1
Modified residuei612PhosphoserineCombined sources1
Modified residuei617Omega-N-methylarginineCombined sources1
Modified residuei632Omega-N-methylarginineCombined 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

Phosphorylated by TBK1; the phosphorylation is required to synergize with TBK1 in IFNB induction. Phosphorylated by IKBKE at Ser-102 after ssRNA viral infection; enhances the induction of INFB promoter by IRF3. The cytoplasmic form is highly phosphorylated in the G1/S phase and much lower phosphorylated in G2/M.3 Publications

Keywords - PTMi

Acetylation, Isopeptide bond, Methylation, Phosphoprotein, Ubl conjugation

Proteomic databases

Encyclopedia of Proteome Dynamics

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EPDi
O00571

jPOST - Japan Proteome Standard Repository/Database

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jPOSTi
O00571

MassIVE - Mass Spectrometry Interactive Virtual Environment

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MassIVEi
O00571

MaxQB - The MaxQuant DataBase

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MaxQBi
O00571

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

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PaxDbi
O00571

PeptideAtlas

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PeptideAtlasi
O00571

PRoteomics IDEntifications database

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PRIDEi
O00571

ProteomicsDB: a multi-organism proteome resource

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ProteomicsDBi
47982 [O00571-1]
47983 [O00571-2]

2D gel databases

REPRODUCTION-2DPAGE

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REPRODUCTION-2DPAGEi
IPI00215637

Two-dimensional polyacrylamide gel electrophoresis database from the Geneva University Hospital

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SWISS-2DPAGEi
O00571

PTM databases

CarbonylDB database of protein carbonylation sites

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CarbonylDBi
O00571

iPTMnet integrated resource for PTMs in systems biology context

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iPTMneti
O00571

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

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PhosphoSitePlusi
O00571

SwissPalm database of S-palmitoylation events

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SwissPalmi
O00571

<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 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

Regulated by the cell cycle. Maximally expressed din the cytoplasm uring G1/S phase and decreased expression during G2/M phase.1 Publication

Gene expression databases

Bgee dataBase for Gene Expression Evolution

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Bgeei
ENSG00000215301 Expressed in 243 organ(s), highest expression level in substantia nigra

ExpressionAtlas, Differential and Baseline Expression

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ExpressionAtlasi
O00571 baseline and differential

Genevisible search portal to normalized and curated expression data from Genevestigator

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Genevisiblei
O00571 HS

Organism-specific databases

Human Protein Atlas

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HPAi
HPA001648
HPA005631
HPA059585

<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

Binds RNA as a monomer at low DDX3X concentrations and as a dimer at high DDX3X concentrations (PubMed:27546789).

Interacts with XPO1, TDRD3, PABPC1, NXF1, EIF3C, MAVS, DDX58 and NCAPH (PubMed:15507209, PubMed:18632687, PubMed:18596238, PubMed:20127681, PubMed:21170385, PubMed:21730191, PubMed:21883093, PubMed:22323517, PubMed:22872150).

Interacts with DDX5; the interaction is regulated by the phosphorylation status of both proteins (PubMed:22034099).

Interacts with EIF4E; DDX3X competes with EIF4G1/EIF4G3 for interaction with EIF4E (PubMed:17667941, PubMed:21883093).

Interacts with IKBKE; the interaction is direct, found to be induced upon virus infection (PubMed:20375222, PubMed:20657822, PubMed:23478265).

Interacts (when phosphorylated at Ser-102) with IRF3; the interaction allows the phosphorylation and activation of IRF3 by IKBKE (PubMed:23478265).

Interacts with TBK1 (PubMed:20375222). Associates with the eukaryotic translation initiation factor 3 (eIF-3) complex (PubMed:18628297). Associates with the 40S ribosome (PubMed:22323517).

Identified in a mRNP complex, at least composed of DHX9, DDX3X, ELAVL1, HNRNPU, IGF2BP1, ILF3, PABPC1, PCBP2, PTBP2, STAU1, STAU2, SYNCRIP and YBX1 (PubMed:19029303).

Interacts with SP1 (PubMed:16818630).

Interacts with GSK3A, GSK3B and TNFRSF10B (PubMed:18846110).

Interacts with XPO1 (PubMed:15507209).

Interacts with CSNK1E; the interaction enhances CSNK1E recruitment to DVL2 (PubMed:23413191).

Interacts with DHX33; the interaction is independent of RNA (PubMed:26100019).

Interacts with ERCC6 (PubMed:26030138).

23 Publications

(Microbial infection) Interacts with HCV core protein.

1 Publication

(Microbial infection) Interacts with vaccinia virus (VACV) protein K7.

2 Publications

(Microbial infection) Interacts with HIV-1 Rev.

1 Publication

(Microbial infection) Interacts with Venezuelan equine encephalitis virus non-structural protein 3.

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
108020, 281 interactors

CORUM comprehensive resource of mammalian protein complexes

More...
CORUMi
O00571

Database of interacting proteins

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DIPi
DIP-27551N

The Eukaryotic Linear Motif resource for Functional Sites in Proteins

More...
ELMi
O00571

Protein interaction database and analysis system

More...
IntActi
O00571, 125 interactors

Molecular INTeraction database

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MINTi
O00571

STRING: functional protein association networks

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STRINGi
9606.ENSP00000382840

Chemistry databases

BindingDB database of measured binding affinities

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BindingDBi
O00571

<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

1662
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

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SMRi
O00571

Database of comparative protein structure models

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ModBasei
Search...

Protein Data Bank in Europe - Knowledge Base

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PDBe-KBi
Search...

Miscellaneous databases

Relative evolutionary importance of amino acids within a protein sequence

More...
EvolutionaryTracei
O00571

<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>Domaini211 – 403Helicase ATP-bindingPROSITE-ProRule annotationAdd BLAST193
Domaini414 – 575Helicase C-terminalPROSITE-ProRule annotationAdd BLAST162

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>Regioni2 – 139Required for TBK1 and IKBKE-dependent IFN-beta activationAdd BLAST138
Regioni2 – 100Interaction with EIF4EAdd BLAST99
Regioni81 – 90Required for interaction with VACV protein K710
Regioni100 – 662Interaction with GSK3B1 PublicationAdd BLAST563
Regioni100 – 110Required for interaction with IKBKEAdd BLAST11
Regioni250 – 259Involved in stimulation of ATPase activity by DNA and RNA, nucleic acid binding and unwinding and HIV-1 replication10
Regioni260 – 517Necessary for interaction with XPO11 PublicationAdd BLAST258

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>Motifi180 – 208Q motifAdd BLAST29
Motifi347 – 350DEAD box4

Compositional bias

Feature keyPosition(s)DescriptionActionsGraphical viewLength
<p>This subsection of the ‘Family and Domains’ section describes the position of regions of compositional bias within the protein and the particular amino acids that are over-represented within those regions.<p><a href='/help/compbias' target='_top'>More...</a></p>Compositional biasi582 – 662Gly/Ser-richAdd BLAST81

<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

Phylogenomic databases

evolutionary genealogy of genes: Non-supervised Orthologous Groups

More...
eggNOGi
KOG0335 Eukaryota
ENOG410XNTI LUCA

Ensembl GeneTree

More...
GeneTreei
ENSGT00940000154443

InParanoid: Eukaryotic Ortholog Groups

More...
InParanoidi
O00571

KEGG Orthology (KO)

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KOi
K11594

Database of Orthologous Groups

More...
OrthoDBi
595675at2759

Database for complete collections of gene phylogenies

More...
PhylomeDBi
O00571

TreeFam database of animal gene trees

More...
TreeFami
TF300364

Family and domain databases

Integrated resource of protein families, domains and functional sites

More...
InterProi
View protein in InterPro
IPR011545 DEAD/DEAH_box_helicase_dom
IPR014001 Helicase_ATP-bd
IPR001650 Helicase_C
IPR027417 P-loop_NTPase
IPR000629 RNA-helicase_DEAD-box_CS
IPR014014 RNA_helicase_DEAD_Q_motif

Pfam protein domain database

More...
Pfami
View protein in Pfam
PF00270 DEAD, 1 hit
PF00271 Helicase_C, 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, 1 hit

PROSITE; a protein domain and family database

More...
PROSITEi
View protein in PROSITE
PS00039 DEAD_ATP_HELICASE, 1 hit
PS51192 HELICASE_ATP_BIND_1, 1 hit
PS51194 HELICASE_CTER, 1 hit
PS51195 Q_MOTIF, 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>. 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_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.

<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 in its mature form or if it represents the precursor.<p><a href='/help/sequence_processing' target='_top'>More...</a></p>Sequence processingi: The displayed sequence is further processed into a mature form.

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 25 potential isoforms that are computationally mapped.Show allAlign All

Isoform 1 (identifier: O00571-1) [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
MSHVAVENAL GLDQQFAGLD LNSSDNQSGG STASKGRYIP PHLRNREATK
60 70 80 90 100
GFYDKDSSGW SSSKDKDAYS SFGSRSDSRG KSSFFSDRGS GSRGRFDDRG
110 120 130 140 150
RSDYDGIGSR GDRSGFGKFE RGGNSRWCDK SDEDDWSKPL PPSERLEQEL
160 170 180 190 200
FSGGNTGINF EKYDDIPVEA TGNNCPPHIE SFSDVEMGEI IMGNIELTRY
210 220 230 240 250
TRPTPVQKHA IPIIKEKRDL MACAQTGSGK TAAFLLPILS QIYSDGPGEA
260 270 280 290 300
LRAMKENGRY GRRKQYPISL VLAPTRELAV QIYEEARKFS YRSRVRPCVV
310 320 330 340 350
YGGADIGQQI RDLERGCHLL VATPGRLVDM MERGKIGLDF CKYLVLDEAD
360 370 380 390 400
RMLDMGFEPQ IRRIVEQDTM PPKGVRHTMM FSATFPKEIQ MLARDFLDEY
410 420 430 440 450
IFLAVGRVGS TSENITQKVV WVEESDKRSF LLDLLNATGK DSLTLVFVET
460 470 480 490 500
KKGADSLEDF LYHEGYACTS IHGDRSQRDR EEALHQFRSG KSPILVATAV
510 520 530 540 550
AARGLDISNV KHVINFDLPS DIEEYVHRIG RTGRVGNLGL ATSFFNERNI
560 570 580 590 600
NITKDLLDLL VEAKQEVPSW LENMAYEHHY KGSSRGRSKS SRFSGGFGAR
610 620 630 640 650
DYRQSSGASS SSFSSSRASS SRSGGGGHGS SRGFGGGGYG GFYNSDGYGG
660
NYNSQGVDWW GN
Length:662
Mass (Da):73,243
Last modified:January 23, 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:i7074D2B8A6EBBF09
GO
Isoform 2 (identifier: O00571-2) [UniParc]FASTAAdd to basket

The sequence of this isoform differs from the canonical sequence as follows:
     35-51: KGRYIPPHLRNREATKG → S

Note: No experimental confirmation available.
Show »
Length:646
Mass (Da):71,355
Checksum:iA8E9EB966FC6C617
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 are 25 potential isoforms mapped to this entry.BLASTAlignShow allAdd to basket
EntryEntry nameProtein names
Gene namesLengthAnnotation
A0A0D9SF53A0A0D9SF53_HUMAN
ATP-dependent RNA helicase DDX3X
DDX3X
733Annotation 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>
A0A0D9SFB3A0A0D9SFB3_HUMAN
ATP-dependent RNA helicase DDX3X
DDX3X
640Annotation 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>
A0A2R8Y645A0A2R8Y645_HUMAN
ATP-dependent RNA helicase DDX3X
DDX3X
716Annotation 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>
A0A087WVZ1A0A087WVZ1_HUMAN
ATP-dependent RNA helicase DDX3X
DDX3X
189Annotation score:

Annotation score:1 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>
A0A2R8Y7T2A0A2R8Y7T2_HUMAN
ATP-dependent RNA helicase DDX3X
DDX3X
476Annotation score:

Annotation score:1 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>
A0A2R8YFS5A0A2R8YFS5_HUMAN
ATP-dependent RNA helicase DDX3X
DDX3X
661Annotation score:

Annotation score:1 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>
A0A2R8YDT5A0A2R8YDT5_HUMAN
ATP-dependent RNA helicase DDX3X
DDX3X
475Annotation score:

Annotation score:1 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>
A0A0D9SG12A0A0D9SG12_HUMAN
ATP-dependent RNA helicase DDX3X
DDX3X
647Annotation score:

Annotation score:1 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>
A0A2R8Y4A4A0A2R8Y4A4_HUMAN
ATP-dependent RNA helicase DDX3X
DDX3X
662Annotation score:

Annotation score:1 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>
A0A2R8Y5G6A0A2R8Y5G6_HUMAN
ATP-dependent RNA helicase DDX3X
DDX3X
622Annotation score:

Annotation score:1 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>
There are more potential isoformsShow all

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 conflicti50K → R in AAC51830 (PubMed:9381176).Curated1
Sequence conflicti50K → R in AAC51829 (PubMed:9381176).Curated1

Natural variant

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Natural variantiVAR_075731214I → T in MRX102; loss-of-function mutation affecting regulation of Wnt signaling. 1 Publication1
Natural variantiVAR_075732233A → V in MRX102. 1 PublicationCorresponds to variant dbSNP:rs796052223Ensembl.1
Natural variantiVAR_075733233Missing in MRX102. 1 Publication1
Natural variantiVAR_075734235L → P in MRX102. 1 PublicationCorresponds to variant dbSNP:rs796052224Ensembl.1
Natural variantiVAR_035839294R → T in a breast cancer sample; somatic mutation. 1 Publication1
Natural variantiVAR_075735300V → F in MRX102. 1 Publication1
Natural variantiVAR_075736326R → H in MRX102; loss-of-function mutation affecting regulation of Wnt signaling. 1 PublicationCorresponds to variant dbSNP:rs797045025EnsemblClinVar.1
Natural variantiVAR_075737351R → Q in MRX102. 1 PublicationCorresponds to variant dbSNP:rs1057518707EnsemblClinVar.1
Natural variantiVAR_075738362R → C in MRX102. 1 PublicationCorresponds to variant dbSNP:rs797045026EnsemblClinVar.1
Natural variantiVAR_075739376R → C in MRX102; loss-of-function mutation affecting regulation of Wnt signaling. 1 PublicationCorresponds to variant dbSNP:rs796052231EnsemblClinVar.1
Natural variantiVAR_075740392L → P in MRX102. 1 PublicationCorresponds to variant dbSNP:rs796052232Ensembl.1
Natural variantiVAR_075741417Q → P in MRX102. 1 PublicationCorresponds to variant dbSNP:rs796052233Ensembl.1
Natural variantiVAR_075742475R → G in MRX102. 1 PublicationCorresponds to variant dbSNP:rs1064794574EnsemblClinVar.1
Natural variantiVAR_075743480R → S in MRX102. 1 Publication1
Natural variantiVAR_075744488R → H in MRX102. 1 PublicationCorresponds to variant dbSNP:rs796052235EnsemblClinVar.1
Natural variantiVAR_075745507I → T in MRX102; loss-of-function mutation affecting regulation of Wnt signaling. 1 PublicationCorresponds to variant dbSNP:rs797045024EnsemblClinVar.1
Natural variantiVAR_075746509N → I in MRX102. 1 Publication