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Protein

Eukaryotic initiation factor 4A-III

Gene

EIF4A3

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

ATP-dependent RNA helicase (PubMed:16170325). Involved in pre-mRNA splicing as component of the spliceosome (PubMed:11991638, PubMed:22961380, PubMed:28502770, PubMed:28076346). Core component of the splicing-dependent multiprotein exon junction complex (EJC) deposited at splice junctions on mRNAs. The EJC is a dynamic structure consisting of core proteins and several peripheral nuclear and cytoplasmic associated factors that join the complex only transiently either during EJC assembly or during subsequent mRNA metabolism. The EJC marks the position of the exon-exon junction in the mature mRNA for the gene expression machinery and the core components remain bound to spliced mRNAs throughout all stages of mRNA metabolism thereby influencing downstream processes including nuclear mRNA export, subcellular mRNA localization, translation efficiency and nonsense-mediated mRNA decay (NMD). Its RNA-dependent ATPase and RNA-helicase activities are induced by CASC3, but abolished in presence of the MAGOH-RBM8A heterodimer, thereby trapping the ATP-bound EJC core onto spliced mRNA in a stable conformation. The inhibition of ATPase activity by the MAGOH-RBM8A heterodimer increases the RNA-binding affinity of the EJC. Involved in translational enhancement of spliced mRNAs after formation of the 80S ribosome complex. Binds spliced mRNA in sequence-independent manner, 20-24 nucleotides upstream of mRNA exon-exon junctions. Shows higher affinity for single-stranded RNA in an ATP-bound core EJC complex than after the ATP is hydrolyzed. Involved in the splicing modulation of BCL2L1/Bcl-X (and probably other apoptotic genes); specifically inhibits formation of proapoptotic isoforms such as Bcl-X(S); the function is different from the established EJC assembly (PubMed:22203037). Involved in craniofacial development (PubMed:24360810).11 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

<p>This subsection of the ‘Function’ section describes regulatory mechanisms for enzymes, transporters or microbial transcription factors, and reports the components which regulate (by activation or inhibition) the reaction.<p><a href='/help/activity_regulation' target='_top'>More...</a></p>Activity regulationi

The ATPase activity is increased some 4-fold in the presence of RNA.1 Publication

Sites

Feature keyPosition(s)DescriptionActionsGraphical viewLength
<p>This subsection of the ‘Function’ section describes the interaction between a single amino acid and another chemical entity. Priority is given to the annotation of physiological ligands.<p><a href='/help/binding' target='_top'>More...</a></p>Binding sitei60ATP; via carbonyl oxygenCombined sources3 Publications1
Binding sitei65ATPCombined sources3 Publications1
Binding sitei342ATPCombined sources3 Publications1

Regions

Feature keyPosition(s)DescriptionActionsGraphical viewLength
<p>This subsection of the ‘Function’ section describes a region in the protein which binds nucleotide phosphates. It always involves more than one amino acid and includes all residues involved in nucleotide-binding.<p><a href='/help/np_bind' target='_top'>More...</a></p>Nucleotide bindingi85 – 90ATPCombined sources3 Publications6
Nucleotide bindingi367 – 371ATPCombined sources3 Publications5

<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 functionHelicase, Hydrolase, RNA-binding
Biological processmRNA processing, mRNA splicing, mRNA transport, Nonsense-mediated mRNA decay, rRNA processing, Translation regulation, Transport
LigandATP-binding, Nucleotide-binding

Enzyme and pathway databases

BRENDA Comprehensive Enzyme Information System

More...
BRENDAi
3.6.4.13 2681

Reactome - a knowledgebase of biological pathways and processes

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Reactomei
R-HSA-109688 Cleavage of Growing Transcript in the Termination Region
R-HSA-1169408 ISG15 antiviral mechanism
R-HSA-159236 Transport of Mature mRNA derived from an Intron-Containing Transcript
R-HSA-429947 Deadenylation of mRNA
R-HSA-72163 mRNA Splicing - Major Pathway
R-HSA-72187 mRNA 3'-end processing
R-HSA-9010553 Regulation of expression of SLITs and ROBOs
R-HSA-975957 Nonsense Mediated Decay (NMD) enhanced by the Exon Junction Complex (EJC)

Protein family/group databases

Transport Classification Database

More...
TCDBi
3.A.18.1.1 the nuclear mrna exporter (mrna-e) 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:
Eukaryotic initiation factor 4A-III (EC:3.6.4.133 Publications)
Short name:
eIF-4A-III
Short name:
eIF4A-III
Alternative name(s):
ATP-dependent RNA helicase DDX48
ATP-dependent RNA helicase eIF4A-3
DEAD box protein 48
Eukaryotic initiation factor 4A-like NUK-34
Eukaryotic translation initiation factor 4A isoform 3
Nuclear matrix protein 265
Short name:
NMP 265
Short name:
hNMP 265
Cleaved into the following chain:
<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:EIF4A3
Synonyms:DDX48, KIAA0111
<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 17

Organism-specific databases

Eukaryotic Pathogen Database Resources

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EuPathDBi
HostDB:ENSG00000141543.9

Human Gene Nomenclature Database

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HGNCi
HGNC:18683 EIF4A3

Online Mendelian Inheritance in Man (OMIM)

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MIMi
608546 gene

neXtProt; the human protein knowledge platform

More...
neXtProti
NX_P38919

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

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

Keywords - Cellular componenti

Cytoplasm, Nucleus, Spliceosome

<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

Richieri-Costa-Pereira syndrome (RCPS)1 Publication
The disease is caused by mutations affecting the gene represented in this entry. EIF4A3 mutations resulting in Richieri-Costa-Pereira syndrome include a repeat expansion of 18 or 20 nucleotides in the 5' untranslated region. Affected individuals have 14 to 16 repeats, while healthy individuals have 3 to 12 repeats (PubMed:24360810).1 Publication
Disease descriptionA syndrome characterized by a unique pattern of anomalies consisting of microstomia, micrognathia, abnormal fusion of mandible, cleft palate/Robin sequence, absence of central lower incisors, minor ears anomalies, hypoplastic first ray, abnormal tibiae, hypoplastic halluces, and clubfeet. Learning disability is also a common finding.
See also OMIM:268305
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_071090270D → G in RCPS. 1 PublicationCorresponds to variant dbSNP:rs587777204EnsemblClinVar.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>Mutagenesisi88K → A: ATPase activity is not increased by the presence of CASC3. Does not prevent EJC formation. Prevents the EJC disassembly. 1 Publication1
Mutagenesisi270D → K: Loss of CWC22-binding and loss of incorporation into EJCs; when associated with K-273. 1 Publication1
Mutagenesisi273D → K: Loss of CWC22-binding and loss of incorporation into EJCs; when associated with K-270. 1 Publication1
Mutagenesisi276 – 277TI → GD: Loss of CWC22-binding and loss of incorporation into EJCs. 1 Publication2
Mutagenesisi301 – 303NFT → LAG: Loss of CWC22-binding and loss of incorporation into EJCs. 1 Publication3
Mutagenesisi334T → V: Reduced incorporation into EJCs. 1 Publication1
Mutagenesisi401D → K: Loss of incorporation into EJCs; when associated with R-402. 1 Publication1
Mutagenesisi402E → R: Loss of incorporation into EJCs; when associated with K-401. 1 Publication1

Keywords - Diseasei

Disease mutation

Organism-specific databases

DisGeNET

More...
DisGeNETi
9775

MalaCards human disease database

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MalaCardsi
EIF4A3
MIMi268305 phenotype

Open Targets

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OpenTargetsi
ENSG00000141543

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

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Orphaneti
3102 Richieri Costa-Pereira syndrome

The Pharmacogenetics and Pharmacogenomics Knowledge Base

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PharmGKBi
PA162384945

Polymorphism and mutation databases

BioMuta curated single-nucleotide variation and disease association database

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BioMutai
EIF4A3

Domain mapping of disease mutations (DMDM)

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DMDMi
20532400

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

Molecule processing

Feature keyPosition(s)DescriptionActionsGraphical viewLength
<p>This subsection of the ‘PTM / Processing’ section describes the extent of a polypeptide chain in the mature protein following processing.<p><a href='/help/chain' target='_top'>More...</a></p>ChainiPRO_00004232671 – 411Eukaryotic initiation factor 4A-IIIAdd BLAST411
<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 methionineiRemoved; alternateCombined sources1 Publication
ChainiPRO_00000549422 – 411Eukaryotic initiation factor 4A-III, N-terminally processedAdd BLAST410

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 residuei1N-acetylmethionineCombined sources1
Modified residuei2N-acetylalanine; in Eukaryotic initiation factor 4A-III, N-terminally processedCombined sources1 Publication1
Modified residuei10PhosphoserineBy similarity1
Modified residuei12PhosphoserineCombined 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-linki19Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO2)Combined sources
Modified residuei124N6-acetyllysineBy similarity1
Cross-linki152Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO2)By similarity
Modified residuei163PhosphothreonineCombined sources1
Modified residuei198N6-acetyllysineBy similarity1
Modified residuei296N6-acetyllysineCombined sources1
Cross-linki314Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO2)Combined sources
Modified residuei321N6-acetyllysineCombined sources1
Cross-linki374Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO2)By similarity
Cross-linki382Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO2)Combined sources

Keywords - PTMi

Acetylation, Isopeptide bond, Phosphoprotein, Ubl conjugation

Proteomic databases

Encyclopedia of Proteome Dynamics

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EPDi
P38919

MaxQB - The MaxQuant DataBase

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MaxQBi
P38919

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

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PaxDbi
P38919

PeptideAtlas

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PeptideAtlasi
P38919

PRoteomics IDEntifications database

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PRIDEi
P38919

ProteomicsDB human proteome resource

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ProteomicsDBi
55305

2D gel databases

REPRODUCTION-2DPAGE

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REPRODUCTION-2DPAGEi
IPI00009328

PTM databases

iPTMnet integrated resource for PTMs in systems biology context

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iPTMneti
P38919

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

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PhosphoSitePlusi
P38919

SwissPalm database of S-palmitoylation events

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SwissPalmi
P38919

<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

Ubiquitously expressed.1 Publication

Gene expression databases

Bgee dataBase for Gene Expression Evolution

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Bgeei
ENSG00000141543 Expressed in 237 organ(s), highest expression level in right adrenal gland

CleanEx database of gene expression profiles

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CleanExi
HS_EIF4A3

ExpressionAtlas, Differential and Baseline Expression

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ExpressionAtlasi
P38919 baseline and differential

Genevisible search portal to normalized and curated expression data from Genevestigator

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Genevisiblei
P38919 HS

Organism-specific databases

Human Protein Atlas

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HPAi
HPA021878

<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

Identified in the spliceosome C complex (PubMed:11991638, PubMed:22961380, PubMed:28502770, PubMed:28076346). Part of the mRNA splicing-dependent exon junction complex (EJC) complex; the core complex contains CASC3, EIF4A3, MAGOH and RBM8A. Interacts with CASC3, MAGOH, NXF1, RBM8A and ALYREF/THOC4. May interact with NOM1. Interacts with POLDIP3. Interacts with CWC22 and PRPF19 in an RNA-independent manner. Direct interaction with CWC22 is mediated by the helicase C-terminal domain. Full interaction with CWC22 occurs only when EIF4A3 is not part of the EJC and prevents EIF4A3 binding to RNA. Interacts with NCBP3 (PubMed:26382858).13 Publications

<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

Protein-protein interaction databases

The Biological General Repository for Interaction Datasets (BioGrid)

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BioGridi
115119, 276 interactors

ComplexPortal: manually curated resource of macromolecular complexes

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ComplexPortali
CPX-1941 Exon junction core complex, MAGOH variant
CPX-682 Exon junction core complex, MAGOHB variant

CORUM comprehensive resource of mammalian protein complexes

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CORUMi
P38919

Database of interacting proteins

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DIPi
DIP-33218N

Protein interaction database and analysis system

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IntActi
P38919, 184 interactors

Molecular INTeraction database

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MINTi
P38919

STRING: functional protein association networks

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STRINGi
9606.ENSP00000269349

<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

1411
Legend: HelixTurnBeta strandPDB Structure known for this area
Show more details

3D structure databases

Protein Model Portal of the PSI-Nature Structural Biology Knowledgebase

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ProteinModelPortali
P38919

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

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SMRi
P38919

Database of comparative protein structure models

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ModBasei
Search...

MobiDB: a database of protein disorder and mobility annotations

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MobiDBi
Search...

Miscellaneous databases

Relative evolutionary importance of amino acids within a protein sequence

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EvolutionaryTracei
P38919

<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>Domaini69 – 239Helicase ATP-bindingPROSITE-ProRule annotationAdd BLAST171
Domaini250 – 411Helicase C-terminalPROSITE-ProRule annotationAdd BLAST162

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>Motifi38 – 66Q motifAdd BLAST29
Motifi187 – 190DEAD boxCurated4

<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

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eggNOGi
KOG0327 Eukaryota
COG0513 LUCA

Ensembl GeneTree

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GeneTreei
ENSGT00940000155037

The HOGENOM Database of Homologous Genes from Fully Sequenced Organisms

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HOGENOMi
HOG000268797

The HOVERGEN Database of Homologous Vertebrate Genes

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HOVERGENi
HBG107989

InParanoid: Eukaryotic Ortholog Groups

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InParanoidi
P38919

KEGG Orthology (KO)

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KOi
K13025

Identification of Orthologs from Complete Genome Data

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OMAi
DEMPVNA

Database of Orthologous Groups

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OrthoDBi
EOG091G07OI

Database for complete collections of gene phylogenies

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PhylomeDBi
P38919

TreeFam database of animal gene trees

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TreeFami
TF300466

Family and domain databases

Conserved Domains Database

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CDDi
cd00079 HELICc, 1 hit

Integrated resource of protein families, domains and functional sites

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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

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

Simple Modular Architecture Research Tool; a protein domain database

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

Superfamily database of structural and functional annotation

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SUPFAMi
SSF52540 SSF52540, 1 hit

PROSITE; a protein domain and family database

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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>.<p><a href='/help/sequences_section' target='_top'>More...</a></p>Sequence (1+)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 has 1 described isoform and 1 potential isoform that is computationally mapped.Show allAlign All

P38919-1 [UniParc]FASTAAdd to basket
« Hide
        10         20         30         40         50
MATTATMATS GSARKRLLKE EDMTKVEFET SEEVDVTPTF DTMGLREDLL
60 70 80 90 100
RGIYAYGFEK PSAIQQRAIK QIIKGRDVIA QSQSGTGKTA TFSISVLQCL
110 120 130 140 150
DIQVRETQAL ILAPTRELAV QIQKGLLALG DYMNVQCHAC IGGTNVGEDI
160 170 180 190 200
RKLDYGQHVV AGTPGRVFDM IRRRSLRTRA IKMLVLDEAD EMLNKGFKEQ
210 220 230 240 250
IYDVYRYLPP ATQVVLISAT LPHEILEMTN KFMTDPIRIL VKRDELTLEG
260 270 280 290 300
IKQFFVAVER EEWKFDTLCD LYDTLTITQA VIFCNTKRKV DWLTEKMREA
310 320 330 340 350
NFTVSSMHGD MPQKERESIM KEFRSGASRV LISTDVWARG LDVPQVSLII
360 370 380 390 400
NYDLPNNREL YIHRIGRSGR YGRKGVAINF VKNDDIRILR DIEQYYSTQI
410
DEMPMNVADL I
Length:411
Mass (Da):46,871
Last modified:January 23, 2007 - v4
<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:i3A21888CA96CA5EA
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
I3L3H2I3L3H2_HUMAN
Eukaryotic initiation factor 4A-III
EIF4A3
390Annotation 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>

<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 BAA04879 differs from that shown. Reason: Erroneous initiation. Translation N-terminally shortened.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 conflicti210P → S in CAA56074 (Ref. 1) Curated1
Sequence conflicti370R → Q in CAA56074 (Ref. 1) Curated1

Natural variant

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Natural variantiVAR_071090270D → G in RCPS. 1 PublicationCorresponds to variant dbSNP:rs587777204EnsemblClinVar.1

Sequence databases

Select the link destinations:

EMBL nucleotide sequence database

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EMBLi

GenBank nucleotide sequence database

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GenBanki

DNA Data Bank of Japan; a nucleotide sequence database

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DDBJi
Links Updated
X79538 mRNA Translation: CAA56074.1
D21853 mRNA Translation: BAA04879.2 Different initiation.
AK290608 mRNA Translation: BAF83297.1
CR456750 mRNA Translation: CAG33031.1
AC087741 Genomic DNA No translation available.
CH471099 Genomic DNA Translation: EAW89584.1
BC003662 mRNA Translation: AAH03662.1
BC004386 mRNA Translation: AAH04386.1
BC011151 mRNA Translation: AAH11151.1

The Consensus CDS (CCDS) project

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CCDSi
CCDS11767.1

Protein sequence database of the Protein Information Resource

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PIRi
S45142

NCBI Reference Sequences

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RefSeqi
NP_055555.1, NM_014740.3

UniGene gene-oriented nucleotide sequence clusters

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UniGenei
Hs.389649

Genome annotation databases

Ensembl eukaryotic genome annotation project

More...
Ensembli
ENST00000269349; ENSP00000269349; ENSG00000141543
ENST00000647795; ENSP00000497661; ENSG00000141543
ENST00000649764; ENSP00000497641; ENSG00000141543

Database of genes from NCBI RefSeq genomes

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GeneIDi
9775

KEGG: Kyoto Encyclopedia of Genes and Genomes

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KEGGi
hsa:9775

UCSC genome browser

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UCSCi
uc002jxs.3 human

<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
X79538 mRNA Translation: CAA56074.1
D21853 mRNA Translation: BAA04879.2 Different initiation.
AK290608 mRNA Translation: BAF83297.1
CR456750 mRNA Translation: CAG33031.1
AC087741 Genomic DNA No translation available.
CH471099 Genomic DNA Translation: EAW89584.1
BC003662 mRNA Translation: AAH03662.1
BC004386 mRNA Translation: AAH04386.1
BC011151 mRNA Translation: AAH11151.1
CCDSiCCDS11767.1
PIRiS45142
RefSeqiNP_055555.1, NM_014740.3
UniGeneiHs.389649

3D structure databases

Select the link destinations:

Protein Data Bank Europe

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PDBei

Protein Data Bank RCSB

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RCSB PDBi

Protein Data Bank Japan

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PDBji
Links Updated
PDB entryMethodResolution (Å)ChainPositionsPDBsum
2HXYX-ray3.30A/B/C/D23-411[»]
2HYIX-ray2.30C/I1-411[»]
2J0QX-ray3.20A/B2-411[»]
2J0SX-ray2.21A2-411[»]
2J0UX-ray3.00A/B38-411[»]
2XB2X-ray3.40A/X1-411[»]
3EX7X-ray2.30C/H1-411[»]
4C9BX-ray2.00A1-411[»]
5MQFelectron microscopy5.90p1-411[»]
5XJCelectron microscopy3.60u1-411[»]
5YZGelectron microscopy4.10u1-411[»]
ProteinModelPortaliP38919
SMRiP38919
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi115119, 276 interactors
ComplexPortaliCPX-1941 Exon junction core complex, MAGOH variant
CPX-682 Exon junction core complex, MAGOHB variant
CORUMiP38919
DIPiDIP-33218N
IntActiP38919, 184 interactors
MINTiP38919
STRINGi9606.ENSP00000269349

Protein family/group databases

TCDBi3.A.18.1.1 the nuclear mrna exporter (mrna-e) family

PTM databases

iPTMnetiP38919
PhosphoSitePlusiP38919
SwissPalmiP38919

Polymorphism and mutation databases

BioMutaiEIF4A3
DMDMi20532400

2D gel databases

REPRODUCTION-2DPAGEiIPI00009328

Proteomic databases

EPDiP38919
MaxQBiP38919
PaxDbiP38919
PeptideAtlasiP38919
PRIDEiP38919
ProteomicsDBi55305

Protocols and materials databases

The DNASU plasmid repository

More...
DNASUi
9775
Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsembliENST00000269349; ENSP00000269349; ENSG00000141543
ENST00000647795; ENSP00000497661; ENSG00000141543
ENST00000649764; ENSP00000497641; ENSG00000141543
GeneIDi9775
KEGGihsa:9775
UCSCiuc002jxs.3 human

Organism-specific databases

Comparative Toxicogenomics Database

More...
CTDi
9775
DisGeNETi9775
EuPathDBiHostDB:ENSG00000141543.9

GeneCards: human genes, protein and diseases

More...
GeneCardsi
EIF4A3
HGNCiHGNC:18683 EIF4A3
HPAiHPA021878
MalaCardsiEIF4A3
MIMi268305 phenotype
608546 gene
neXtProtiNX_P38919
OpenTargetsiENSG00000141543
Orphaneti3102 Richieri Costa-Pereira syndrome
PharmGKBiPA162384945

Human Unidentified Gene-Encoded large proteins database

More...
HUGEi
Search...

GenAtlas: human gene database

More...
GenAtlasi
Search...

Phylogenomic databases

eggNOGiKOG0327 Eukaryota
COG0513 LUCA
GeneTreeiENSGT00940000155037
HOGENOMiHOG000268797
HOVERGENiHBG107989
InParanoidiP38919
KOiK13025
OMAiDEMPVNA
OrthoDBiEOG091G07OI
PhylomeDBiP38919
TreeFamiTF300466

Enzyme and pathway databases

BRENDAi3.6.4.13 2681
ReactomeiR-HSA-109688 Cleavage of Growing Transcript in the Termination Region
R-HSA-1169408 ISG15 antiviral mechanism
R-HSA-159236 Transport of Mature mRNA derived from an Intron-Containing Transcript
R-HSA-429947 Deadenylation of mRNA
R-HSA-72163 mRNA Splicing - Major Pathway
R-HSA-72187 mRNA 3'-end processing
R-HSA-9010553 Regulation of expression of SLITs and ROBOs
R-HSA-975957 Nonsense Mediated Decay (NMD) enhanced by the Exon Junction Complex (EJC)

Miscellaneous databases

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

More...
ChiTaRSi
EIF4A3 human
EvolutionaryTraceiP38919

The Gene Wiki collection of pages on human genes and proteins

More...
GeneWikii
EIF4A3

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

More...
GenomeRNAii
9775

Protein Ontology

More...
PROi
PR:P38919

The Stanford Online Universal Resource for Clones and ESTs

More...
SOURCEi
Search...

Gene expression databases

BgeeiENSG00000141543 Expressed in 237 organ(s), highest expression level in right adrenal gland
CleanExiHS_EIF4A3
ExpressionAtlasiP38919 baseline and differential
GenevisibleiP38919 HS

Family and domain databases

CDDicd00079 HELICc, 1 hit
InterProiView 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
PfamiView protein in Pfam
PF00270 DEAD, 1 hit
PF00271 Helicase_C, 1 hit
SMARTiView protein in SMART
SM00487 DEXDc, 1 hit
SM00490 HELICc, 1 hit
SUPFAMiSSF52540 SSF52540, 1 hit
PROSITEiView 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

ProtoNet; Automatic hierarchical classification of proteins

More...
ProtoNeti
Search...

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

<p>This subsection of the ‘Entry information’ section provides a mnemonic identifier for a UniProtKB entry, but it is not a stable identifier. Each reviewed entry is assigned a unique entry name upon integration into UniProtKB/Swiss-Prot.<p><a href='/help/entry_name' target='_top'>More...</a></p>Entry nameiIF4A3_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: P38919
Secondary accession number(s): Q15033, Q6IBQ2, Q96A18
<p>This subsection of the ‘Entry information’ section shows the date of integration of the entry into UniProtKB, the date of the last sequence update and the date of the last annotation modification (‘Last modified’). The version number for both the entry and the <a href="http://www.uniprot.org/help/canonical_and_isoforms">canonical sequence</a> are also displayed.<p><a href='/help/entry_history' target='_top'>More...</a></p>Entry historyiIntegrated into UniProtKB/Swiss-Prot: February 1, 1995
Last sequence update: January 23, 2007
Last modified: December 5, 2018
This is version 217 of the entry and version 4 of the sequence. See complete history.
<p>This subsection of the ‘Entry information’ section indicates whether the entry has been manually annotated and reviewed by UniProtKB curators or not, in other words, if the entry belongs to the Swiss-Prot section of UniProtKB (<strong>reviewed</strong>) or to the computer-annotated TrEMBL section (<strong>unreviewed</strong>).<p><a href='/help/entry_status' target='_top'>More...</a></p>Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program
DisclaimerAny medical or genetic information present in this entry is provided for research, educational and informational purposes only. It is not in any way intended to be used as a substitute for professional medical advice, diagnosis, treatment or care.

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

Keywords - Technical termi

3D-structure, Complete proteome, Direct protein sequencing, Reference proteome

Documents

  1. PDB cross-references
    Index of Protein Data Bank (PDB) cross-references
  2. SIMILARITY comments
    Index of protein domains and families
  3. Human chromosome 17
    Human chromosome 17: entries, gene names and cross-references to MIM
  4. Translation initiation factors
    List of translation initiation factor entries
  5. Human polymorphisms and disease mutations
    Index of human polymorphisms and disease mutations
  6. Human entries with polymorphisms or disease mutations
    List of human entries with polymorphisms or disease mutations
  7. MIM cross-references
    Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot
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