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P38919

- IF4A3_HUMAN

UniProt

P38919 - IF4A3_HUMAN

Protein

Eukaryotic initiation factor 4A-III

Gene

EIF4A3

Organism
Homo sapiens (Human)
Status
Reviewed - Annotation score: 5 out of 5- Experimental evidence at protein leveli
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    • History
      Entry version 170 (01 Oct 2014)
      Sequence version 4 (23 Jan 2007)
      Previous versions | rss
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    Functioni

    ATP-dependent RNA helicase. 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. Involved in craniofacial development.7 Publications

    Catalytic activityi

    ATP + H2O = ADP + phosphate.

    Enzyme regulationi

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

    Sites

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Binding sitei60 – 601ATP; via carbonyl oxygen
    Binding sitei65 – 651ATP
    Binding sitei342 – 3421ATP

    Regions

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Nucleotide bindingi85 – 906ATP
    Nucleotide bindingi367 – 3715ATP

    GO - Molecular functioni

    1. ATP binding Source: HGNC
    2. ATP-dependent RNA helicase activity Source: HGNC
    3. mRNA binding Source: UniProtKB
    4. poly(A) binding Source: HGNC
    5. poly(A) RNA binding Source: UniProtKB
    6. protein binding Source: UniProtKB

    GO - Biological processi

    1. ATP catabolic process Source: GOC
    2. cytokine-mediated signaling pathway Source: Reactome
    3. embryonic cranial skeleton morphogenesis Source: UniProtKB
    4. gene expression Source: Reactome
    5. mRNA metabolic process Source: Reactome
    6. mRNA splicing, via spliceosome Source: UniProtKB
    7. mRNA transport Source: UniProtKB-KW
    8. negative regulation of translation Source: HGNC
    9. nuclear-transcribed mRNA catabolic process, deadenylation-dependent decay Source: Reactome
    10. nuclear-transcribed mRNA catabolic process, nonsense-mediated decay Source: UniProtKB
    11. nuclear-transcribed mRNA poly(A) tail shortening Source: Reactome
    12. positive regulation of translation Source: UniProtKB
    13. RNA metabolic process Source: Reactome
    14. rRNA processing Source: UniProtKB-KW

    Keywords - Molecular functioni

    Helicase, Hydrolase

    Keywords - Biological processi

    mRNA processing, mRNA splicing, mRNA transport, Nonsense-mediated mRNA decay, rRNA processing, Translation regulation, Transport

    Keywords - Ligandi

    ATP-binding, Nucleotide-binding, RNA-binding

    Enzyme and pathway databases

    ReactomeiREACT_115831. ISG15 antiviral mechanism.
    REACT_20514. Deadenylation of mRNA.
    REACT_75822. Nonsense Mediated Decay (NMD) enhanced by the Exon Junction Complex (EJC).

    Protein family/group databases

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

    Names & Taxonomyi

    Protein namesi
    Recommended name:
    Eukaryotic initiation factor 4A-III (EC:3.6.4.13)
    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:
    Gene namesi
    Name:EIF4A3
    Synonyms:DDX48, KIAA0111
    OrganismiHomo sapiens (Human)
    Taxonomic identifieri9606 [NCBI]
    Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
    ProteomesiUP000005640: Chromosome 17

    Organism-specific databases

    HGNCiHGNC:18683. EIF4A3.

    Subcellular locationi

    Nucleus. Nucleus speckle. Cytoplasm
    Note: Nucleocytoplasmic shuttling protein. Travels to the cytoplasm as part of the exon junction complex (EJC) bound to mRNA. Detected in dendritic layer as well as the nuclear and cytoplasmic (somatic) compartments of neurons. Colocalizes with STAU1 and FMR1 in dendrites By similarity.By similarity

    GO - Cellular componenti

    1. catalytic step 2 spliceosome Source: UniProtKB
    2. cytoplasm Source: HGNC
    3. cytosol Source: Reactome
    4. exon-exon junction complex Source: UniProtKB
    5. membrane Source: UniProtKB
    6. nuclear speck Source: UniProtKB-SubCell
    7. nucleus Source: HPA

    Keywords - Cellular componenti

    Cytoplasm, Nucleus, Spliceosome

    Pathology & Biotechi

    Involvement in diseasei

    Richieri-Costa-Pereira syndrome (RCPS) [MIM:268305]: A 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.1 Publication
    Note: 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
    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Natural varianti270 – 2701D → G in RCPS. 1 Publication
    VAR_071090

    Mutagenesis

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Mutagenesisi88 – 881K → A: ATPase activity is not induced in presence of CASC3. Does not prevent EJC formation. Prevents the EJC disassembly. 2 Publications
    Mutagenesisi270 – 2701D → K: Loss of CWC22-binding and loss of incorporation into EJCs; when associated with K-273. 2 Publications
    Mutagenesisi273 – 2731D → K: Loss of CWC22-binding and loss of incorporation into EJCs; when associated with K-270. 2 Publications
    Mutagenesisi276 – 2772TI → GD: Loss of CWC22-binding and loss of incorporation into EJCs. 1 Publication
    Mutagenesisi301 – 3033NFT → LAG: Loss of CWC22-binding and loss of incorporation into EJCs. 1 Publication
    Mutagenesisi334 – 3341T → V: Reduced incorporation into EJCs. 2 Publications
    Mutagenesisi401 – 4011D → K: Loss of incorporation into EJCs; when associated with R-402. 2 Publications
    Mutagenesisi402 – 4021E → R: Loss of incorporation into EJCs; when associated with K-401. 2 Publications

    Keywords - Diseasei

    Disease mutation

    Organism-specific databases

    MIMi268305. phenotype.
    Orphaneti3102. Richieri Costa-Pereira syndrome.
    PharmGKBiPA162384945.

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Chaini1 – 411411Eukaryotic initiation factor 4A-IIIPRO_0000423267Add
    BLAST
    Initiator methioninei1 – 11Removed; alternate5 Publications
    Chaini2 – 411410Eukaryotic initiation factor 4A-III, N-terminally processedPRO_0000054942Add
    BLAST

    Amino acid modifications

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Modified residuei1 – 11N-acetylmethionine2 Publications
    Modified residuei2 – 21N-acetylalanine; in Eukaryotic initiation factor 4A-III, N-terminally processed7 Publications
    Modified residuei12 – 121Phosphoserine2 Publications
    Modified residuei163 – 1631Phosphothreonine2 Publications
    Modified residuei296 – 2961N6-acetyllysine1 Publication
    Modified residuei321 – 3211N6-acetyllysine1 Publication

    Keywords - PTMi

    Acetylation, Phosphoprotein

    Proteomic databases

    MaxQBiP38919.
    PaxDbiP38919.
    PeptideAtlasiP38919.
    PRIDEiP38919.

    2D gel databases

    REPRODUCTION-2DPAGEIPI00009328.

    PTM databases

    PhosphoSiteiP38919.

    Expressioni

    Tissue specificityi

    Ubiquitously expressed.1 Publication

    Gene expression databases

    ArrayExpressiP38919.
    BgeeiP38919.
    CleanExiHS_EIF4A3.
    GenevestigatoriP38919.

    Organism-specific databases

    HPAiHPA021878.

    Interactioni

    Subunit structurei

    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. Identified in the spliceosome C complex. 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.10 Publications

    Binary interactionsi

    WithEntry#Exp.IntActNotes
    CASC3O152347EBI-299104,EBI-299118
    CWC22Q9HCG83EBI-299104,EBI-373289
    MAGOHP6132620EBI-299104,EBI-299134
    RBM8AQ9Y5S921EBI-299104,EBI-447231
    THRAP3Q9Y2W12EBI-299104,EBI-352039
    UPF3BQ9BZI77EBI-299104,EBI-372780

    Protein-protein interaction databases

    BioGridi115119. 228 interactions.
    DIPiDIP-33218N.
    IntActiP38919. 134 interactions.
    MINTiMINT-1460615.
    STRINGi9606.ENSP00000269349.

    Structurei

    Secondary structure

    1
    411
    Legend: HelixTurnBeta strand
    Show more details
    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Helixi23 – 253
    Beta strandi28 – 325
    Helixi40 – 423
    Helixi47 – 5610
    Helixi65 – 739
    Beta strandi78 – 814
    Beta strandi84 – 863
    Helixi88 – 9811
    Beta strandi102 – 1043
    Beta strandi109 – 1124
    Helixi116 – 12914
    Turni130 – 1345
    Beta strandi137 – 1393
    Helixi143 – 1453
    Helixi146 – 15510
    Beta strandi158 – 1625
    Helixi164 – 1729
    Beta strandi183 – 1864
    Helixi189 – 1957
    Helixi198 – 2069
    Beta strandi213 – 2197
    Helixi223 – 23210
    Beta strandi237 – 2415
    Helixi243 – 2453
    Beta strandi251 – 26010
    Helixi261 – 2633
    Helixi264 – 27411
    Beta strandi278 – 2836
    Helixi287 – 29913
    Beta strandi304 – 3074
    Beta strandi309 – 3113
    Helixi313 – 32412
    Beta strandi329 – 3335
    Helixi335 – 3373
    Beta strandi338 – 3403
    Beta strandi346 – 3538
    Beta strandi356 – 3583
    Helixi360 – 3656
    Beta strandi367 – 3693
    Helixi370 – 3723
    Beta strandi375 – 3828
    Helixi383 – 3853
    Helixi386 – 39611
    Beta strandi400 – 4023
    Helixi405 – 4106

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    Links Updated
    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[»]
    ProteinModelPortaliP38919.
    SMRiP38919. Positions 21-411.
    ModBaseiSearch...
    MobiDBiSearch...

    Miscellaneous databases

    EvolutionaryTraceiP38919.

    Family & Domainsi

    Domains and Repeats

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Domaini69 – 239171Helicase ATP-bindingPROSITE-ProRule annotationAdd
    BLAST
    Domaini250 – 411162Helicase C-terminalPROSITE-ProRule annotationAdd
    BLAST

    Motif

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Motifi38 – 6629Q motifAdd
    BLAST
    Motifi187 – 1904DEAD box

    Sequence similaritiesi

    Contains 1 helicase ATP-binding domain.PROSITE-ProRule annotation
    Contains 1 helicase C-terminal domain.PROSITE-ProRule annotation

    Phylogenomic databases

    eggNOGiCOG0513.
    HOGENOMiHOG000268797.
    HOVERGENiHBG107989.
    InParanoidiP38919.
    KOiK13025.
    OMAiHANIQAH.
    PhylomeDBiP38919.
    TreeFamiTF300466.

    Family and domain databases

    Gene3Di3.40.50.300. 2 hits.
    InterProiIPR011545. DNA/RNA_helicase_DEAD/DEAH_N.
    IPR014001. Helicase_ATP-bd.
    IPR001650. Helicase_C.
    IPR027417. P-loop_NTPase.
    IPR000629. RNA-helicase_DEAD-box_CS.
    IPR014014. RNA_helicase_DEAD_Q_motif.
    [Graphical view]
    PfamiPF00270. DEAD. 1 hit.
    PF00271. Helicase_C. 1 hit.
    [Graphical view]
    SMARTiSM00487. DEXDc. 1 hit.
    SM00490. HELICc. 1 hit.
    [Graphical view]
    SUPFAMiSSF52540. SSF52540. 1 hit.
    PROSITEiPS00039. DEAD_ATP_HELICASE. 1 hit.
    PS51192. HELICASE_ATP_BIND_1. 1 hit.
    PS51194. HELICASE_CTER. 1 hit.
    PS51195. Q_MOTIF. 1 hit.
    [Graphical view]

    Sequencei

    Sequence statusi: Complete.

    Sequence processingi: The displayed sequence is further processed into a mature form.

    P38919-1 [UniParc]FASTAAdd to Basket

    « Hide

    MATTATMATS GSARKRLLKE EDMTKVEFET SEEVDVTPTF DTMGLREDLL    50
    RGIYAYGFEK PSAIQQRAIK QIIKGRDVIA QSQSGTGKTA TFSISVLQCL 100
    DIQVRETQAL ILAPTRELAV QIQKGLLALG DYMNVQCHAC IGGTNVGEDI 150
    RKLDYGQHVV AGTPGRVFDM IRRRSLRTRA IKMLVLDEAD EMLNKGFKEQ 200
    IYDVYRYLPP ATQVVLISAT LPHEILEMTN KFMTDPIRIL VKRDELTLEG 250
    IKQFFVAVER EEWKFDTLCD LYDTLTITQA VIFCNTKRKV DWLTEKMREA 300
    NFTVSSMHGD MPQKERESIM KEFRSGASRV LISTDVWARG LDVPQVSLII 350
    NYDLPNNREL YIHRIGRSGR YGRKGVAINF VKNDDIRILR DIEQYYSTQI 400
    DEMPMNVADL I 411
    Length:411
    Mass (Da):46,871
    Last modified:January 23, 2007 - v4
    Checksum:i3A21888CA96CA5EA
    GO

    Sequence cautioni

    The sequence BAA04879.2 differs from that shown. Reason: Erroneous initiation. Translation N-terminally shortened.

    Experimental Info

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Sequence conflicti210 – 2101P → S in CAA56074. 1 PublicationCurated
    Sequence conflicti370 – 3701R → Q in CAA56074. 1 PublicationCurated

    Natural variant

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Natural varianti270 – 2701D → G in RCPS. 1 Publication
    VAR_071090

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    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.

    Genome annotation databases

    EnsembliENST00000269349; ENSP00000269349; ENSG00000141543.
    GeneIDi9775.
    KEGGihsa:9775.
    UCSCiuc002jxs.3. human.

    Polymorphism databases

    DMDMi20532400.

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    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 .
    CCDSi CCDS11767.1.
    PIRi S45142.
    RefSeqi NP_055555.1. NM_014740.3.
    UniGenei Hs.389649.

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    Links Updated
    Entry Method Resolution (Å) Chain Positions PDBsum
    2HXY X-ray 3.30 A/B/C/D 23-411 [» ]
    2HYI X-ray 2.30 C/I 1-411 [» ]
    2J0Q X-ray 3.20 A/B 2-411 [» ]
    2J0S X-ray 2.21 A 2-411 [» ]
    2J0U X-ray 3.00 A/B 38-411 [» ]
    2XB2 X-ray 3.40 A/X 1-411 [» ]
    3EX7 X-ray 2.30 C/H 1-411 [» ]
    4C9B X-ray 2.00 A 1-411 [» ]
    ProteinModelPortali P38919.
    SMRi P38919. Positions 21-411.
    ModBasei Search...
    MobiDBi Search...

    Protein-protein interaction databases

    BioGridi 115119. 228 interactions.
    DIPi DIP-33218N.
    IntActi P38919. 134 interactions.
    MINTi MINT-1460615.
    STRINGi 9606.ENSP00000269349.

    Protein family/group databases

    TCDBi 3.A.18.1.1. the nuclear mrna exporter (mrna-e) family.

    PTM databases

    PhosphoSitei P38919.

    Polymorphism databases

    DMDMi 20532400.

    2D gel databases

    REPRODUCTION-2DPAGE IPI00009328.

    Proteomic databases

    MaxQBi P38919.
    PaxDbi P38919.
    PeptideAtlasi P38919.
    PRIDEi P38919.

    Protocols and materials databases

    DNASUi 9775.
    Structural Biology Knowledgebase Search...

    Genome annotation databases

    Ensembli ENST00000269349 ; ENSP00000269349 ; ENSG00000141543 .
    GeneIDi 9775.
    KEGGi hsa:9775.
    UCSCi uc002jxs.3. human.

    Organism-specific databases

    CTDi 9775.
    GeneCardsi GC17M078109.
    HGNCi HGNC:18683. EIF4A3.
    HPAi HPA021878.
    MIMi 268305. phenotype.
    608546. gene.
    neXtProti NX_P38919.
    Orphaneti 3102. Richieri Costa-Pereira syndrome.
    PharmGKBi PA162384945.
    HUGEi Search...
    GenAtlasi Search...

    Phylogenomic databases

    eggNOGi COG0513.
    HOGENOMi HOG000268797.
    HOVERGENi HBG107989.
    InParanoidi P38919.
    KOi K13025.
    OMAi HANIQAH.
    PhylomeDBi P38919.
    TreeFami TF300466.

    Enzyme and pathway databases

    Reactomei REACT_115831. ISG15 antiviral mechanism.
    REACT_20514. Deadenylation of mRNA.
    REACT_75822. Nonsense Mediated Decay (NMD) enhanced by the Exon Junction Complex (EJC).

    Miscellaneous databases

    ChiTaRSi EIF4A3. human.
    EvolutionaryTracei P38919.
    GeneWikii EIF4A3.
    GenomeRNAii 9775.
    NextBioi 36802.
    PROi P38919.
    SOURCEi Search...

    Gene expression databases

    ArrayExpressi P38919.
    Bgeei P38919.
    CleanExi HS_EIF4A3.
    Genevestigatori P38919.

    Family and domain databases

    Gene3Di 3.40.50.300. 2 hits.
    InterProi IPR011545. DNA/RNA_helicase_DEAD/DEAH_N.
    IPR014001. Helicase_ATP-bd.
    IPR001650. Helicase_C.
    IPR027417. P-loop_NTPase.
    IPR000629. RNA-helicase_DEAD-box_CS.
    IPR014014. RNA_helicase_DEAD_Q_motif.
    [Graphical view ]
    Pfami PF00270. DEAD. 1 hit.
    PF00271. Helicase_C. 1 hit.
    [Graphical view ]
    SMARTi SM00487. DEXDc. 1 hit.
    SM00490. HELICc. 1 hit.
    [Graphical view ]
    SUPFAMi SSF52540. SSF52540. 1 hit.
    PROSITEi PS00039. DEAD_ATP_HELICASE. 1 hit.
    PS51192. HELICASE_ATP_BIND_1. 1 hit.
    PS51194. HELICASE_CTER. 1 hit.
    PS51195. Q_MOTIF. 1 hit.
    [Graphical view ]
    ProtoNeti Search...

    Publicationsi

    1. "Cloning and sequencing of a putative human translation initiation factor with similarity to initiation factor 4AII."
      Leffers H., Wiemann S., Ansorge W.
      Submitted (JUN-1994) to the EMBL/GenBank/DDBJ databases
      Cited for: NUCLEOTIDE SEQUENCE [MRNA].
      Tissue: Skin.
    2. "Prediction of the coding sequences of unidentified human genes. III. The coding sequences of 40 new genes (KIAA0081-KIAA0120) deduced by analysis of cDNA clones from human cell line KG-1."
      Nagase T., Miyajima N., Tanaka A., Sazuka T., Seki N., Sato S., Tabata S., Ishikawa K., Kawarabayasi Y., Kotani H., Nomura N.
      DNA Res. 2:37-43(1995) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
      Tissue: Bone marrow.
    3. "Complete sequencing and characterization of 21,243 full-length human cDNAs."
      Ota T., Suzuki Y., Nishikawa T., Otsuki T., Sugiyama T., Irie R., Wakamatsu A., Hayashi K., Sato H., Nagai K., Kimura K., Makita H., Sekine M., Obayashi M., Nishi T., Shibahara T., Tanaka T., Ishii S.
      , Yamamoto J., Saito K., Kawai Y., Isono Y., Nakamura Y., Nagahari K., Murakami K., Yasuda T., Iwayanagi T., Wagatsuma M., Shiratori A., Sudo H., Hosoiri T., Kaku Y., Kodaira H., Kondo H., Sugawara M., Takahashi M., Kanda K., Yokoi T., Furuya T., Kikkawa E., Omura Y., Abe K., Kamihara K., Katsuta N., Sato K., Tanikawa M., Yamazaki M., Ninomiya K., Ishibashi T., Yamashita H., Murakawa K., Fujimori K., Tanai H., Kimata M., Watanabe M., Hiraoka S., Chiba Y., Ishida S., Ono Y., Takiguchi S., Watanabe S., Yosida M., Hotuta T., Kusano J., Kanehori K., Takahashi-Fujii A., Hara H., Tanase T.-O., Nomura Y., Togiya S., Komai F., Hara R., Takeuchi K., Arita M., Imose N., Musashino K., Yuuki H., Oshima A., Sasaki N., Aotsuka S., Yoshikawa Y., Matsunawa H., Ichihara T., Shiohata N., Sano S., Moriya S., Momiyama H., Satoh N., Takami S., Terashima Y., Suzuki O., Nakagawa S., Senoh A., Mizoguchi H., Goto Y., Shimizu F., Wakebe H., Hishigaki H., Watanabe T., Sugiyama A., Takemoto M., Kawakami B., Yamazaki M., Watanabe K., Kumagai A., Itakura S., Fukuzumi Y., Fujimori Y., Komiyama M., Tashiro H., Tanigami A., Fujiwara T., Ono T., Yamada K., Fujii Y., Ozaki K., Hirao M., Ohmori Y., Kawabata A., Hikiji T., Kobatake N., Inagaki H., Ikema Y., Okamoto S., Okitani R., Kawakami T., Noguchi S., Itoh T., Shigeta K., Senba T., Matsumura K., Nakajima Y., Mizuno T., Morinaga M., Sasaki M., Togashi T., Oyama M., Hata H., Watanabe M., Komatsu T., Mizushima-Sugano J., Satoh T., Shirai Y., Takahashi Y., Nakagawa K., Okumura K., Nagase T., Nomura N., Kikuchi H., Masuho Y., Yamashita R., Nakai K., Yada T., Nakamura Y., Ohara O., Isogai T., Sugano S.
      Nat. Genet. 36:40-45(2004) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
      Tissue: Heart.
    4. "Cloning of human full open reading frames in Gateway(TM) system entry vector (pDONR201)."
      Ebert L., Schick M., Neubert P., Schatten R., Henze S., Korn B.
      Submitted (JUN-2004) to the EMBL/GenBank/DDBJ databases
      Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
    5. "DNA sequence of human chromosome 17 and analysis of rearrangement in the human lineage."
      Zody M.C., Garber M., Adams D.J., Sharpe T., Harrow J., Lupski J.R., Nicholson C., Searle S.M., Wilming L., Young S.K., Abouelleil A., Allen N.R., Bi W., Bloom T., Borowsky M.L., Bugalter B.E., Butler J., Chang J.L.
      , Chen C.-K., Cook A., Corum B., Cuomo C.A., de Jong P.J., DeCaprio D., Dewar K., FitzGerald M., Gilbert J., Gibson R., Gnerre S., Goldstein S., Grafham D.V., Grocock R., Hafez N., Hagopian D.S., Hart E., Norman C.H., Humphray S., Jaffe D.B., Jones M., Kamal M., Khodiyar V.K., LaButti K., Laird G., Lehoczky J., Liu X., Lokyitsang T., Loveland J., Lui A., Macdonald P., Major J.E., Matthews L., Mauceli E., McCarroll S.A., Mihalev A.H., Mudge J., Nguyen C., Nicol R., O'Leary S.B., Osoegawa K., Schwartz D.C., Shaw-Smith C., Stankiewicz P., Steward C., Swarbreck D., Venkataraman V., Whittaker C.A., Yang X., Zimmer A.R., Bradley A., Hubbard T., Birren B.W., Rogers J., Lander E.S., Nusbaum C.
      Nature 440:1045-1049(2006) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    6. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    7. "The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC)."
      The MGC Project Team
      Genome Res. 14:2121-2127(2004) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
      Tissue: Lymph, Placenta and Skin.
    8. Bienvenut W.V., Kanor S., Tissot J.-D., Quadroni M.
      Submitted (MAY-2006) to UniProtKB
      Cited for: PROTEIN SEQUENCE OF 2-14, CLEAVAGE OF INITIATOR METHIONINE, ACETYLATION AT ALA-2, IDENTIFICATION BY MASS SPECTROMETRY.
      Tissue: T-cell.
    9. Lubec G., Vishwanath V.
      Submitted (MAR-2007) to UniProtKB
      Cited for: PROTEIN SEQUENCE OF 340-358, IDENTIFICATION BY MASS SPECTROMETRY.
      Tissue: Brain and Cajal-Retzius cell.
    10. "A human common nuclear matrix protein homologous to eukaryotic translation initiation factor 4A."
      Holzmann K., Gerner C., Poeltl A., Schaefer R., Obrist P., Ensinger C., Grimm R., Sauermann G.
      Biochem. Biophys. Res. Commun. 267:339-344(2000) [PubMed] [Europe PMC] [Abstract]
      Cited for: PARTIAL PROTEIN SEQUENCE, SUBCELLULAR LOCATION, TISSUE SPECIFICITY.
      Tissue: Leukocyte.
    11. "Purification and characterization of native spliceosomes suitable for three-dimensional structural analysis."
      Jurica M.S., Licklider L.J., Gygi S.P., Grigorieff N., Moore M.J.
      RNA 8:426-439(2002) [PubMed] [Europe PMC] [Abstract]
      Cited for: IDENTIFICATION BY MASS SPECTROMETRY, IDENTIFICATION IN THE SPLICEOSOMAL C COMPLEX.
    12. "eIF4AIII binds spliced mRNA in the exon junction complex and is essential for nonsense-mediated decay."
      Shibuya T., Tange T.O., Sonenberg N., Moore M.J.
      Nat. Struct. Mol. Biol. 11:346-351(2004) [PubMed] [Europe PMC] [Abstract]
      Cited for: FUNCTION IN MRNA SPLICING AND NONSENSE-MEDIATED MRNA DECAY, INTERACTION WITH MAGOH AND RBM8A, RNA-BINDING.
    13. "eIF4A3 is a novel component of the exon junction complex."
      Chan C.C., Dostie J., Diem M.D., Feng W., Mann M., Rappsilber J., Dreyfuss G.
      RNA 10:200-209(2004) [PubMed] [Europe PMC] [Abstract]
      Cited for: IDENTIFICATION BY MASS SPECTROMETRY, IDENTIFICATION IN THE EXON JUNCTION COMPLEX, INTERACTION WITH NXF1 AND ALYREF/THOC4, RNA-BINDING, SUBCELLULAR LOCATION.
    14. "Identification of NOM1, a nucleolar, eIF4A binding protein encoded within the chromosome 7q36 breakpoint region targeted in cases of pediatric acute myeloid leukemia."
      Simmons H.M., Ruis B.L., Kapoor M., Hudacek A.W., Conklin K.F.
      Gene 347:137-145(2005) [PubMed] [Europe PMC] [Abstract]
      Cited for: POSSIBLE INTERACTION WITH NOM1.
    15. "Exon-junction complex components specify distinct routes of nonsense-mediated mRNA decay with differential cofactor requirements."
      Gehring N.H., Kunz J.B., Neu-Yilik G., Breit S., Viegas M.H., Hentze M.W., Kulozik A.E.
      Mol. Cell 20:65-75(2005) [PubMed] [Europe PMC] [Abstract]
      Cited for: FUNCTION.
    16. "The exon junction core complex is locked onto RNA by inhibition of eIF4AIII ATPase activity."
      Ballut L., Marchadier B., Baguet A., Tomasetto C., Seraphin B., Le Hir H.
      Nat. Struct. Mol. Biol. 12:861-869(2005) [PubMed] [Europe PMC] [Abstract]
      Cited for: FUNCTION, IDENTIFICATION IN THE CORE EXON JUNCTION COMPLEX, INTERACTION WITH CASC3, MUTAGENESIS OF LYS-88, RNA-BINDING.
    17. "Biochemical analysis of the EJC reveals two new factors and a stable tetrameric protein core."
      Tange T.O., Shibuya T., Jurica M.S., Moore M.J.
      RNA 11:1869-1883(2005) [PubMed] [Europe PMC] [Abstract]
      Cited for: IDENTIFICATION IN THE CORE EXON JUNCTION COMPLEX, IDENTIFICATION IN A MRNA SPLICING-DEPENDENT EXON JUNCTION COMPLEX, IDENTIFICATION BY MASS SPECTROMETRY.
    18. "Global, in vivo, and site-specific phosphorylation dynamics in signaling networks."
      Olsen J.V., Blagoev B., Gnad F., Macek B., Kumar C., Mortensen P., Mann M.
      Cell 127:635-648(2006) [PubMed] [Europe PMC] [Abstract]
      Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
      Tissue: Cervix carcinoma.
    19. "Mutational analysis of human eIF4AIII identifies regions necessary for exon junction complex formation and nonsense-mediated mRNA decay."
      Shibuya T., Tange T.O., Stroupe M.E., Moore M.J.
      RNA 12:360-374(2006) [PubMed] [Europe PMC] [Abstract]
      Cited for: INTERACTION WITH CASC3 AND MAGOH, MUTAGENESIS.
    20. "MLN51 stimulates the RNA-helicase activity of eIF4AIII."
      Noble C.G., Song H.
      PLoS ONE 2:E303-E303(2007) [PubMed] [Europe PMC] [Abstract]
      Cited for: FUNCTION IN ATPASE AND RNA-HELICASE ACTIVITY.
    21. "SKAR links pre-mRNA splicing to mTOR/S6K1-mediated enhanced translation efficiency of spliced mRNAs."
      Ma X.M., Yoon S.O., Richardson C.J., Julich K., Blenis J.
      Cell 133:303-313(2008) [PubMed] [Europe PMC] [Abstract]
      Cited for: INTERACTION WITH POLDIP3.
    22. "Kinase-selective enrichment enables quantitative phosphoproteomics of the kinome across the cell cycle."
      Daub H., Olsen J.V., Bairlein M., Gnad F., Oppermann F.S., Korner R., Greff Z., Keri G., Stemmann O., Mann M.
      Mol. Cell 31:438-448(2008) [PubMed] [Europe PMC] [Abstract]
      Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
      Tissue: Cervix carcinoma.
    23. Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-163, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
      Tissue: Cervix carcinoma.
    24. "Lys-N and trypsin cover complementary parts of the phosphoproteome in a refined SCX-based approach."
      Gauci S., Helbig A.O., Slijper M., Krijgsveld J., Heck A.J., Mohammed S.
      Anal. Chem. 81:4493-4501(2009) [PubMed] [Europe PMC] [Abstract]
      Cited for: ACETYLATION [LARGE SCALE ANALYSIS] AT ALA-2, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    25. "Exon junction complex enhances translation of spliced mRNAs at multiple steps."
      Lee H.C., Choe J., Chi S.G., Kim Y.K.
      Biochem. Biophys. Res. Commun. 384:334-340(2009) [PubMed] [Europe PMC] [Abstract]
      Cited for: FUNCTION IN MRNA TRANSLATION.
    26. Cited for: ACETYLATION [LARGE SCALE ANALYSIS] AT ALA-2, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    27. "Lysine acetylation targets protein complexes and co-regulates major cellular functions."
      Choudhary C., Kumar C., Gnad F., Nielsen M.L., Rehman M., Walther T.C., Olsen J.V., Mann M.
      Science 325:834-840(2009) [PubMed] [Europe PMC] [Abstract]
      Cited for: ACETYLATION [LARGE SCALE ANALYSIS] AT LYS-296 AND LYS-321, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    28. "Quantitative phosphoproteomics reveals widespread full phosphorylation site occupancy during mitosis."
      Olsen J.V., Vermeulen M., Santamaria A., Kumar C., Miller M.L., Jensen L.J., Gnad F., Cox J., Jensen T.S., Nigg E.A., Brunak S., Mann M.
      Sci. Signal. 3:RA3-RA3(2010) [PubMed] [Europe PMC] [Abstract]
      Cited for: ACETYLATION [LARGE SCALE ANALYSIS] AT MET-1 AND ALA-2, PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-12 AND THR-163, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
      Tissue: Cervix carcinoma.
    29. Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    30. "System-wide temporal characterization of the proteome and phosphoproteome of human embryonic stem cell differentiation."
      Rigbolt K.T., Prokhorova T.A., Akimov V., Henningsen J., Johansen P.T., Kratchmarova I., Kassem M., Mann M., Olsen J.V., Blagoev B.
      Sci. Signal. 4:RS3-RS3(2011) [PubMed] [Europe PMC] [Abstract]
      Cited for: ACETYLATION [LARGE SCALE ANALYSIS] AT MET-1 AND ALA-2, PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-12, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    31. "CWC22 connects pre-mRNA splicing and exon junction complex assembly."
      Steckelberg A.L., Boehm V., Gromadzka A.M., Gehring N.H.
      Cell Rep. 2:454-461(2012) [PubMed] [Europe PMC] [Abstract]
      Cited for: INTERACTION WITH CWC22, MUTAGENESIS OF ASP-270; ASP-273; 276-THR-ILE-277 AND 301-ASN--THR-303.
    32. "Proteins associated with the exon junction complex also control the alternative splicing of apoptotic regulators."
      Michelle L., Cloutier A., Toutant J., Shkreta L., Thibault P., Durand M., Garneau D., Gendron D., Lapointe E., Couture S., Le Hir H., Klinck R., Elela S.A., Prinos P., Chabot B.
      Mol. Cell. Biol. 32:954-967(2012) [PubMed] [Europe PMC] [Abstract]
      Cited for: FUNCTION.
    33. "Comparative large-scale characterisation of plant vs. mammal proteins reveals similar and idiosyncratic N-alpha acetylation features."
      Bienvenut W.V., Sumpton D., Martinez A., Lilla S., Espagne C., Meinnel T., Giglione C.
      Mol. Cell. Proteomics 11:M111.015131-M111.015131(2012) [PubMed] [Europe PMC] [Abstract]
      Cited for: ACETYLATION [LARGE SCALE ANALYSIS] AT ALA-2, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    34. "Human CWC22 escorts the helicase eIF4AIII to spliceosomes and promotes exon junction complex assembly."
      Barbosa I., Haque N., Fiorini F., Barrandon C., Tomasetto C., Blanchette M., Le Hir H.
      Nat. Struct. Mol. Biol. 19:983-990(2012) [PubMed] [Europe PMC] [Abstract]
      Cited for: ENZYME REGULATION, INTERACTION WITH CASC3; CWC22; MAGOH; PRPF19 AND RBM8A, SUBCELLULAR LOCATION, MUTAGENESIS OF ASP-401 AND GLU-402.
    35. Cited for: ACETYLATION [LARGE SCALE ANALYSIS] AT ALA-2, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    36. "Human spliceosomal protein CWC22 plays a role in coupling splicing to exon junction complex deposition and nonsense-mediated decay."
      Alexandrov A., Colognori D., Shu M.D., Steitz J.A.
      Proc. Natl. Acad. Sci. U.S.A. 109:21313-21318(2012) [PubMed] [Europe PMC] [Abstract]
      Cited for: INTERACTION WITH CWC22, MUTAGENESIS OF THR-334.
    37. Cited for: FUNCTION, VARIANT RCPS GLY-270.
    38. "The crystal structure of the exon junction complex reveals how it maintains a stable grip on mRNA."
      Bono F., Ebert J., Lorentzen E., Conti E.
      Cell 126:713-725(2006) [PubMed] [Europe PMC] [Abstract]
      Cited for: X-RAY CRYSTALLOGRAPHY (2.21 ANGSTROMS) OF 2-411 IN THE EJC COMPLEX WITH CASC3; MAGOH; RBM8A; AMP-PNP AND POLY URACIL.
    39. "Structure of the exon junction core complex with a trapped DEAD-box ATPase bound to RNA."
      Andersen C.B., Ballut L., Johansen J.S., Chamieh H., Nielsen K.H., Oliveira C.L., Pedersen J.S., Seraphin B., Le Hir H., Andersen G.R.
      Science 313:1968-1972(2006) [PubMed] [Europe PMC] [Abstract]
      Cited for: X-RAY CRYSTALLOGRAPHY (2.3 ANGSTROMS) IN THE EJC COMPLEX WITH CASC3; MAGOH; RBM8A; ADP-NP AND POLY URACIL.
    40. Cited for: X-RAY CRYSTALLOGRAPHY (2.3 ANGSTROMS) IN THE EJC COMPLEX WITH CASC3; MAGOH; RBM8A; TRANSITION STATE ANALOG ADP-ALF3 AND POLY URACIL.

    Entry informationi

    Entry nameiIF4A3_HUMAN
    AccessioniPrimary (citable) accession number: P38919
    Secondary accession number(s): Q15033, Q6IBQ2, Q96A18
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: February 1, 1995
    Last sequence update: January 23, 2007
    Last modified: October 1, 2014
    This is version 170 of the entry and version 4 of the sequence. [Complete history]
    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.

    Miscellaneousi

    Keywords - Technical termi

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

    Documents

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

    External Data

    Dasty 3