IF4A3_HUMAN
ID IF4A3_HUMAN Reviewed; 411 AA.
AC P38919; Q15033; Q6IBQ2; Q96A18;
DT 01-FEB-1995, integrated into UniProtKB/Swiss-Prot.
DT 23-JAN-2007, sequence version 4.
DT 03-AUG-2022, entry version 241.
DE RecName: Full=Eukaryotic initiation factor 4A-III;
DE Short=eIF-4A-III;
DE Short=eIF4A-III;
DE EC=3.6.4.13 {ECO:0000269|PubMed:16170325, ECO:0000269|PubMed:17375189, ECO:0000269|PubMed:22961380};
DE AltName: Full=ATP-dependent RNA helicase DDX48;
DE AltName: Full=ATP-dependent RNA helicase eIF4A-3;
DE AltName: Full=DEAD box protein 48;
DE AltName: Full=Eukaryotic initiation factor 4A-like NUK-34;
DE AltName: Full=Eukaryotic translation initiation factor 4A isoform 3;
DE AltName: Full=Nuclear matrix protein 265;
DE Short=NMP 265;
DE Short=hNMP 265;
DE Contains:
DE RecName: Full=Eukaryotic initiation factor 4A-III, N-terminally processed;
GN Name=EIF4A3; Synonyms=DDX48, KIAA0111;
OS Homo sapiens (Human).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini; Hominidae;
OC Homo.
OX NCBI_TaxID=9606;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA].
RC TISSUE=Skin;
RA Leffers H., Wiemann S., Ansorge W.;
RT "Cloning and sequencing of a putative human translation initiation factor
RT with similarity to initiation factor 4AII.";
RL Submitted (JUN-1994) to the EMBL/GenBank/DDBJ databases.
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC TISSUE=Bone marrow;
RX PubMed=7788527; DOI=10.1093/dnares/2.1.37;
RA Nagase T., Miyajima N., Tanaka A., Sazuka T., Seki N., Sato S., Tabata S.,
RA Ishikawa K., Kawarabayasi Y., Kotani H., Nomura N.;
RT "Prediction of the coding sequences of unidentified human genes. III. The
RT coding sequences of 40 new genes (KIAA0081-KIAA0120) deduced by analysis of
RT cDNA clones from human cell line KG-1.";
RL DNA Res. 2:37-43(1995).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC TISSUE=Heart;
RX PubMed=14702039; DOI=10.1038/ng1285;
RA Ota T., Suzuki Y., Nishikawa T., Otsuki T., Sugiyama T., Irie R.,
RA Wakamatsu A., Hayashi K., Sato H., Nagai K., Kimura K., Makita H.,
RA Sekine M., Obayashi M., Nishi T., Shibahara T., Tanaka T., Ishii S.,
RA Yamamoto J., Saito K., Kawai Y., Isono Y., Nakamura Y., Nagahari K.,
RA Murakami K., Yasuda T., Iwayanagi T., Wagatsuma M., Shiratori A., Sudo H.,
RA Hosoiri T., Kaku Y., Kodaira H., Kondo H., Sugawara M., Takahashi M.,
RA Kanda K., Yokoi T., Furuya T., Kikkawa E., Omura Y., Abe K., Kamihara K.,
RA Katsuta N., Sato K., Tanikawa M., Yamazaki M., Ninomiya K., Ishibashi T.,
RA Yamashita H., Murakawa K., Fujimori K., Tanai H., Kimata M., Watanabe M.,
RA Hiraoka S., Chiba Y., Ishida S., Ono Y., Takiguchi S., Watanabe S.,
RA Yosida M., Hotuta T., Kusano J., Kanehori K., Takahashi-Fujii A., Hara H.,
RA Tanase T.-O., Nomura Y., Togiya S., Komai F., Hara R., Takeuchi K.,
RA Arita M., Imose N., Musashino K., Yuuki H., Oshima A., Sasaki N.,
RA Aotsuka S., Yoshikawa Y., Matsunawa H., Ichihara T., Shiohata N., Sano S.,
RA Moriya S., Momiyama H., Satoh N., Takami S., Terashima Y., Suzuki O.,
RA Nakagawa S., Senoh A., Mizoguchi H., Goto Y., Shimizu F., Wakebe H.,
RA Hishigaki H., Watanabe T., Sugiyama A., Takemoto M., Kawakami B.,
RA Yamazaki M., Watanabe K., Kumagai A., Itakura S., Fukuzumi Y., Fujimori Y.,
RA Komiyama M., Tashiro H., Tanigami A., Fujiwara T., Ono T., Yamada K.,
RA Fujii Y., Ozaki K., Hirao M., Ohmori Y., Kawabata A., Hikiji T.,
RA Kobatake N., Inagaki H., Ikema Y., Okamoto S., Okitani R., Kawakami T.,
RA Noguchi S., Itoh T., Shigeta K., Senba T., Matsumura K., Nakajima Y.,
RA Mizuno T., Morinaga M., Sasaki M., Togashi T., Oyama M., Hata H.,
RA Watanabe M., Komatsu T., Mizushima-Sugano J., Satoh T., Shirai Y.,
RA Takahashi Y., Nakagawa K., Okumura K., Nagase T., Nomura N., Kikuchi H.,
RA Masuho Y., Yamashita R., Nakai K., Yada T., Nakamura Y., Ohara O.,
RA Isogai T., Sugano S.;
RT "Complete sequencing and characterization of 21,243 full-length human
RT cDNAs.";
RL Nat. Genet. 36:40-45(2004).
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RA Ebert L., Schick M., Neubert P., Schatten R., Henze S., Korn B.;
RT "Cloning of human full open reading frames in Gateway(TM) system entry
RT vector (pDONR201).";
RL Submitted (JUN-2004) to the EMBL/GenBank/DDBJ databases.
RN [5]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=16625196; DOI=10.1038/nature04689;
RA Zody M.C., Garber M., Adams D.J., Sharpe T., Harrow J., Lupski J.R.,
RA Nicholson C., Searle S.M., Wilming L., Young S.K., Abouelleil A.,
RA Allen N.R., Bi W., Bloom T., Borowsky M.L., Bugalter B.E., Butler J.,
RA Chang J.L., Chen C.-K., Cook A., Corum B., Cuomo C.A., de Jong P.J.,
RA DeCaprio D., Dewar K., FitzGerald M., Gilbert J., Gibson R., Gnerre S.,
RA Goldstein S., Grafham D.V., Grocock R., Hafez N., Hagopian D.S., Hart E.,
RA Norman C.H., Humphray S., Jaffe D.B., Jones M., Kamal M., Khodiyar V.K.,
RA LaButti K., Laird G., Lehoczky J., Liu X., Lokyitsang T., Loveland J.,
RA Lui A., Macdonald P., Major J.E., Matthews L., Mauceli E., McCarroll S.A.,
RA Mihalev A.H., Mudge J., Nguyen C., Nicol R., O'Leary S.B., Osoegawa K.,
RA Schwartz D.C., Shaw-Smith C., Stankiewicz P., Steward C., Swarbreck D.,
RA Venkataraman V., Whittaker C.A., Yang X., Zimmer A.R., Bradley A.,
RA Hubbard T., Birren B.W., Rogers J., Lander E.S., Nusbaum C.;
RT "DNA sequence of human chromosome 17 and analysis of rearrangement in the
RT human lineage.";
RL Nature 440:1045-1049(2006).
RN [6]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RA Mural R.J., Istrail S., Sutton G.G., Florea L., Halpern A.L., Mobarry C.M.,
RA Lippert R., Walenz B., Shatkay H., Dew I., Miller J.R., Flanigan M.J.,
RA Edwards N.J., Bolanos R., Fasulo D., Halldorsson B.V., Hannenhalli S.,
RA Turner R., Yooseph S., Lu F., Nusskern D.R., Shue B.C., Zheng X.H.,
RA Zhong F., Delcher A.L., Huson D.H., Kravitz S.A., Mouchard L., Reinert K.,
RA Remington K.A., Clark A.G., Waterman M.S., Eichler E.E., Adams M.D.,
RA Hunkapiller M.W., Myers E.W., Venter J.C.;
RL Submitted (JUL-2005) to the EMBL/GenBank/DDBJ databases.
RN [7]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC TISSUE=Lymph, Placenta, and Skin;
RX PubMed=15489334; DOI=10.1101/gr.2596504;
RG The MGC Project Team;
RT "The status, quality, and expansion of the NIH full-length cDNA project:
RT the Mammalian Gene Collection (MGC).";
RL Genome Res. 14:2121-2127(2004).
RN [8]
RP PROTEIN SEQUENCE OF 2-14, CLEAVAGE OF INITIATOR METHIONINE, ACETYLATION AT
RP ALA-2, AND IDENTIFICATION BY MASS SPECTROMETRY.
RC TISSUE=T-cell;
RA Bienvenut W.V., Kanor S., Tissot J.-D., Quadroni M.;
RL Submitted (MAY-2006) to UniProtKB.
RN [9]
RP PROTEIN SEQUENCE OF 340-358, AND IDENTIFICATION BY MASS SPECTROMETRY.
RC TISSUE=Brain, and Cajal-Retzius cell;
RA Lubec G., Vishwanath V.;
RL Submitted (MAR-2007) to UniProtKB.
RN [10]
RP PARTIAL PROTEIN SEQUENCE, SUBCELLULAR LOCATION, AND TISSUE SPECIFICITY.
RC TISSUE=Leukocyte;
RX PubMed=10623621; DOI=10.1006/bbrc.1999.1973;
RA Holzmann K., Gerner C., Poeltl A., Schaefer R., Obrist P., Ensinger C.,
RA Grimm R., Sauermann G.;
RT "A human common nuclear matrix protein homologous to eukaryotic translation
RT initiation factor 4A.";
RL Biochem. Biophys. Res. Commun. 267:339-344(2000).
RN [11]
RP IDENTIFICATION BY MASS SPECTROMETRY, IDENTIFICATION IN THE SPLICEOSOMAL C
RP COMPLEX, FUNCTION, SUBCELLULAR LOCATION, AND SUBUNIT.
RX PubMed=11991638; DOI=10.1017/s1355838202021088;
RA Jurica M.S., Licklider L.J., Gygi S.P., Grigorieff N., Moore M.J.;
RT "Purification and characterization of native spliceosomes suitable for
RT three-dimensional structural analysis.";
RL RNA 8:426-439(2002).
RN [12]
RP FUNCTION IN MRNA SPLICING AND NONSENSE-MEDIATED MRNA DECAY, INTERACTION
RP WITH MAGOH AND RBM8A, AND RNA-BINDING.
RX PubMed=15034551; DOI=10.1038/nsmb750;
RA Shibuya T., Tange T.O., Sonenberg N., Moore M.J.;
RT "eIF4AIII binds spliced mRNA in the exon junction complex and is essential
RT for nonsense-mediated decay.";
RL Nat. Struct. Mol. Biol. 11:346-351(2004).
RN [13]
RP IDENTIFICATION BY MASS SPECTROMETRY, IDENTIFICATION IN THE EXON JUNCTION
RP COMPLEX, INTERACTION WITH NXF1 AND ALYREF/THOC4, RNA-BINDING, AND
RP SUBCELLULAR LOCATION.
RX PubMed=14730019; DOI=10.1261/rna.5230104;
RA Chan C.C., Dostie J., Diem M.D., Feng W., Mann M., Rappsilber J.,
RA Dreyfuss G.;
RT "eIF4A3 is a novel component of the exon junction complex.";
RL RNA 10:200-209(2004).
RN [14]
RP POSSIBLE INTERACTION WITH NOM1.
RX PubMed=15715967; DOI=10.1016/j.gene.2004.12.027;
RA Simmons H.M., Ruis B.L., Kapoor M., Hudacek A.W., Conklin K.F.;
RT "Identification of NOM1, a nucleolar, eIF4A binding protein encoded within
RT the chromosome 7q36 breakpoint region targeted in cases of pediatric acute
RT myeloid leukemia.";
RL Gene 347:137-145(2005).
RN [15]
RP FUNCTION.
RX PubMed=16209946; DOI=10.1016/j.molcel.2005.08.012;
RA Gehring N.H., Kunz J.B., Neu-Yilik G., Breit S., Viegas M.H., Hentze M.W.,
RA Kulozik A.E.;
RT "Exon-junction complex components specify distinct routes of nonsense-
RT mediated mRNA decay with differential cofactor requirements.";
RL Mol. Cell 20:65-75(2005).
RN [16]
RP FUNCTION, CATALYTIC ACTIVITY, IDENTIFICATION IN THE CORE EXON JUNCTION
RP COMPLEX, INTERACTION WITH CASC3, MUTAGENESIS OF LYS-88, AND RNA-BINDING.
RX PubMed=16170325; DOI=10.1038/nsmb990;
RA Ballut L., Marchadier B., Baguet A., Tomasetto C., Seraphin B., Le Hir H.;
RT "The exon junction core complex is locked onto RNA by inhibition of
RT eIF4AIII ATPase activity.";
RL Nat. Struct. Mol. Biol. 12:861-869(2005).
RN [17]
RP IDENTIFICATION IN THE CORE EXON JUNCTION COMPLEX, IDENTIFICATION IN A MRNA
RP SPLICING-DEPENDENT EXON JUNCTION COMPLEX, AND IDENTIFICATION BY MASS
RP SPECTROMETRY.
RX PubMed=16314458; DOI=10.1261/rna.2155905;
RA Tange T.O., Shibuya T., Jurica M.S., Moore M.J.;
RT "Biochemical analysis of the EJC reveals two new factors and a stable
RT tetrameric protein core.";
RL RNA 11:1869-1883(2005).
RN [18]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Cervix carcinoma;
RX PubMed=17081983; DOI=10.1016/j.cell.2006.09.026;
RA Olsen J.V., Blagoev B., Gnad F., Macek B., Kumar C., Mortensen P., Mann M.;
RT "Global, in vivo, and site-specific phosphorylation dynamics in signaling
RT networks.";
RL Cell 127:635-648(2006).
RN [19]
RP INTERACTION WITH CASC3 AND MAGOH, AND MUTAGENESIS.
RX PubMed=16495234; DOI=10.1261/rna.2190706;
RA Shibuya T., Tange T.O., Stroupe M.E., Moore M.J.;
RT "Mutational analysis of human eIF4AIII identifies regions necessary for
RT exon junction complex formation and nonsense-mediated mRNA decay.";
RL RNA 12:360-374(2006).
RN [20]
RP FUNCTION IN ATPASE AND RNA-HELICASE ACTIVITY, AND CATALYTIC ACTIVITY.
RX PubMed=17375189; DOI=10.1371/journal.pone.0000303;
RA Noble C.G., Song H.;
RT "MLN51 stimulates the RNA-helicase activity of eIF4AIII.";
RL PLoS ONE 2:E303-E303(2007).
RN [21]
RP INTERACTION WITH POLDIP3.
RX PubMed=18423201; DOI=10.1016/j.cell.2008.02.031;
RA Ma X.M., Yoon S.O., Richardson C.J., Julich K., Blenis J.;
RT "SKAR links pre-mRNA splicing to mTOR/S6K1-mediated enhanced translation
RT efficiency of spliced mRNAs.";
RL Cell 133:303-313(2008).
RN [22]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Cervix carcinoma;
RX PubMed=18691976; DOI=10.1016/j.molcel.2008.07.007;
RA Daub H., Olsen J.V., Bairlein M., Gnad F., Oppermann F.S., Korner R.,
RA Greff Z., Keri G., Stemmann O., Mann M.;
RT "Kinase-selective enrichment enables quantitative phosphoproteomics of the
RT kinome across the cell cycle.";
RL Mol. Cell 31:438-448(2008).
RN [23]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-163, AND IDENTIFICATION BY
RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Cervix carcinoma;
RX PubMed=18669648; DOI=10.1073/pnas.0805139105;
RA Dephoure N., Zhou C., Villen J., Beausoleil S.A., Bakalarski C.E.,
RA Elledge S.J., Gygi S.P.;
RT "A quantitative atlas of mitotic phosphorylation.";
RL Proc. Natl. Acad. Sci. U.S.A. 105:10762-10767(2008).
RN [24]
RP ACETYLATION [LARGE SCALE ANALYSIS] AT ALA-2, CLEAVAGE OF INITIATOR
RP METHIONINE [LARGE SCALE ANALYSIS], AND IDENTIFICATION BY MASS SPECTROMETRY
RP [LARGE SCALE ANALYSIS].
RX PubMed=19413330; DOI=10.1021/ac9004309;
RA Gauci S., Helbig A.O., Slijper M., Krijgsveld J., Heck A.J., Mohammed S.;
RT "Lys-N and trypsin cover complementary parts of the phosphoproteome in a
RT refined SCX-based approach.";
RL Anal. Chem. 81:4493-4501(2009).
RN [25]
RP FUNCTION IN MRNA TRANSLATION.
RX PubMed=19409878; DOI=10.1016/j.bbrc.2009.04.123;
RA Lee H.C., Choe J., Chi S.G., Kim Y.K.;
RT "Exon junction complex enhances translation of spliced mRNAs at multiple
RT steps.";
RL Biochem. Biophys. Res. Commun. 384:334-340(2009).
RN [26]
RP ACETYLATION [LARGE SCALE ANALYSIS] AT ALA-2, CLEAVAGE OF INITIATOR
RP METHIONINE [LARGE SCALE ANALYSIS], AND IDENTIFICATION BY MASS SPECTROMETRY
RP [LARGE SCALE ANALYSIS].
RX PubMed=19369195; DOI=10.1074/mcp.m800588-mcp200;
RA Oppermann F.S., Gnad F., Olsen J.V., Hornberger R., Greff Z., Keri G.,
RA Mann M., Daub H.;
RT "Large-scale proteomics analysis of the human kinome.";
RL Mol. Cell. Proteomics 8:1751-1764(2009).
RN [27]
RP ACETYLATION [LARGE SCALE ANALYSIS] AT LYS-296 AND LYS-321, AND
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=19608861; DOI=10.1126/science.1175371;
RA Choudhary C., Kumar C., Gnad F., Nielsen M.L., Rehman M., Walther T.C.,
RA Olsen J.V., Mann M.;
RT "Lysine acetylation targets protein complexes and co-regulates major
RT cellular functions.";
RL Science 325:834-840(2009).
RN [28]
RP ACETYLATION [LARGE SCALE ANALYSIS] AT MET-1 AND ALA-2, PHOSPHORYLATION
RP [LARGE SCALE ANALYSIS] AT SER-12 AND THR-163, CLEAVAGE OF INITIATOR
RP METHIONINE [LARGE SCALE ANALYSIS], AND IDENTIFICATION BY MASS SPECTROMETRY
RP [LARGE SCALE ANALYSIS].
RC TISSUE=Cervix carcinoma;
RX PubMed=20068231; DOI=10.1126/scisignal.2000475;
RA Olsen J.V., Vermeulen M., Santamaria A., Kumar C., Miller M.L.,
RA Jensen L.J., Gnad F., Cox J., Jensen T.S., Nigg E.A., Brunak S., Mann M.;
RT "Quantitative phosphoproteomics reveals widespread full phosphorylation
RT site occupancy during mitosis.";
RL Sci. Signal. 3:RA3-RA3(2010).
RN [29]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=21269460; DOI=10.1186/1752-0509-5-17;
RA Burkard T.R., Planyavsky M., Kaupe I., Breitwieser F.P., Buerckstuemmer T.,
RA Bennett K.L., Superti-Furga G., Colinge J.;
RT "Initial characterization of the human central proteome.";
RL BMC Syst. Biol. 5:17-17(2011).
RN [30]
RP ACETYLATION [LARGE SCALE ANALYSIS] AT MET-1 AND ALA-2, PHOSPHORYLATION
RP [LARGE SCALE ANALYSIS] AT SER-12, CLEAVAGE OF INITIATOR METHIONINE [LARGE
RP SCALE ANALYSIS], AND IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE
RP ANALYSIS].
RX PubMed=21406692; DOI=10.1126/scisignal.2001570;
RA Rigbolt K.T., Prokhorova T.A., Akimov V., Henningsen J., Johansen P.T.,
RA Kratchmarova I., Kassem M., Mann M., Olsen J.V., Blagoev B.;
RT "System-wide temporal characterization of the proteome and phosphoproteome
RT of human embryonic stem cell differentiation.";
RL Sci. Signal. 4:RS3-RS3(2011).
RN [31]
RP INTERACTION WITH CWC22, AND MUTAGENESIS OF ASP-270; ASP-273;
RP 276-THR-ILE-277 AND 301-ASN--THR-303.
RX PubMed=22959432; DOI=10.1016/j.celrep.2012.08.017;
RA Steckelberg A.L., Boehm V., Gromadzka A.M., Gehring N.H.;
RT "CWC22 connects pre-mRNA splicing and exon junction complex assembly.";
RL Cell Rep. 2:454-461(2012).
RN [32]
RP FUNCTION.
RX PubMed=22203037; DOI=10.1128/mcb.06130-11;
RA Michelle L., Cloutier A., Toutant J., Shkreta L., Thibault P., Durand M.,
RA Garneau D., Gendron D., Lapointe E., Couture S., Le Hir H., Klinck R.,
RA Elela S.A., Prinos P., Chabot B.;
RT "Proteins associated with the exon junction complex also control the
RT alternative splicing of apoptotic regulators.";
RL Mol. Cell. Biol. 32:954-967(2012).
RN [33]
RP ACETYLATION [LARGE SCALE ANALYSIS] AT ALA-2, CLEAVAGE OF INITIATOR
RP METHIONINE [LARGE SCALE ANALYSIS], AND IDENTIFICATION BY MASS SPECTROMETRY
RP [LARGE SCALE ANALYSIS].
RX PubMed=22223895; DOI=10.1074/mcp.m111.015131;
RA Bienvenut W.V., Sumpton D., Martinez A., Lilla S., Espagne C., Meinnel T.,
RA Giglione C.;
RT "Comparative large-scale characterisation of plant vs. mammal proteins
RT reveals similar and idiosyncratic N-alpha acetylation features.";
RL Mol. Cell. Proteomics 11:M111.015131-M111.015131(2012).
RN [34]
RP FUNCTION, CATALYTIC ACTIVITY, ACTIVITY REGULATION, IDENTIFICATION IN THE
RP SPLICEOSOME C COMPLEX, INTERACTION WITH CASC3; CWC22; MAGOH; PRPF19 AND
RP RBM8A, SUBCELLULAR LOCATION, AND MUTAGENESIS OF ASP-401 AND GLU-402.
RX PubMed=22961380; DOI=10.1038/nsmb.2380;
RA Barbosa I., Haque N., Fiorini F., Barrandon C., Tomasetto C.,
RA Blanchette M., Le Hir H.;
RT "Human CWC22 escorts the helicase eIF4AIII to spliceosomes and promotes
RT exon junction complex assembly.";
RL Nat. Struct. Mol. Biol. 19:983-990(2012).
RN [35]
RP ACETYLATION [LARGE SCALE ANALYSIS] AT ALA-2, CLEAVAGE OF INITIATOR
RP METHIONINE [LARGE SCALE ANALYSIS], AND IDENTIFICATION BY MASS SPECTROMETRY
RP [LARGE SCALE ANALYSIS].
RX PubMed=22814378; DOI=10.1073/pnas.1210303109;
RA Van Damme P., Lasa M., Polevoda B., Gazquez C., Elosegui-Artola A.,
RA Kim D.S., De Juan-Pardo E., Demeyer K., Hole K., Larrea E., Timmerman E.,
RA Prieto J., Arnesen T., Sherman F., Gevaert K., Aldabe R.;
RT "N-terminal acetylome analyses and functional insights of the N-terminal
RT acetyltransferase NatB.";
RL Proc. Natl. Acad. Sci. U.S.A. 109:12449-12454(2012).
RN [36]
RP INTERACTION WITH CWC22, AND MUTAGENESIS OF THR-334.
RX PubMed=23236153; DOI=10.1073/pnas.1219725110;
RA Alexandrov A., Colognori D., Shu M.D., Steitz J.A.;
RT "Human spliceosomal protein CWC22 plays a role in coupling splicing to exon
RT junction complex deposition and nonsense-mediated decay.";
RL Proc. Natl. Acad. Sci. U.S.A. 109:21313-21318(2012).
RN [37]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-12 AND THR-163, AND
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Cervix carcinoma, and Erythroleukemia;
RX PubMed=23186163; DOI=10.1021/pr300630k;
RA Zhou H., Di Palma S., Preisinger C., Peng M., Polat A.N., Heck A.J.,
RA Mohammed S.;
RT "Toward a comprehensive characterization of a human cancer cell
RT phosphoproteome.";
RL J. Proteome Res. 12:260-271(2013).
RN [38]
RP IDENTIFICATION IN THE EXON JUNCTION COMPLEX.
RX PubMed=23917022; DOI=10.4161/rna.25827;
RA Singh K.K., Wachsmuth L., Kulozik A.E., Gehring N.H.;
RT "Two mammalian MAGOH genes contribute to exon junction complex composition
RT and nonsense-mediated decay.";
RL RNA Biol. 10:1291-1298(2013).
RN [39]
RP FUNCTION, AND VARIANT RCPS GLY-270.
RX PubMed=24360810; DOI=10.1016/j.ajhg.2013.11.020;
RA Favaro F.P., Alvizi L., Zechi-Ceide R.M., Bertola D., Felix T.M.,
RA de Souza J., Raskin S., Twigg S.R., Weiner A.M., Armas P., Margarit E.,
RA Calcaterra N.B., Andersen G.R., McGowan S.J., Wilkie A.O.,
RA Richieri-Costa A., de Almeida M.L., Passos-Bueno M.R.;
RT "A noncoding expansion in EIF4A3 causes Richieri-Costa-Pereira syndrome, a
RT craniofacial disorder associated with limb defects.";
RL Am. J. Hum. Genet. 94:120-128(2014).
RN [40]
RP INTERACTION WITH DHX34.
RX PubMed=25220460; DOI=10.1016/j.celrep.2014.08.020;
RA Hug N., Caceres J.F.;
RT "The RNA helicase DHX34 activates NMD by promoting a transition from the
RT surveillance to the decay-inducing complex.";
RL Cell Rep. 8:1845-1856(2014).
RN [41]
RP SUMOYLATION [LARGE SCALE ANALYSIS] AT LYS-19, AND IDENTIFICATION BY MASS
RP SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=25218447; DOI=10.1038/nsmb.2890;
RA Hendriks I.A., D'Souza R.C., Yang B., Verlaan-de Vries M., Mann M.,
RA Vertegaal A.C.;
RT "Uncovering global SUMOylation signaling networks in a site-specific
RT manner.";
RL Nat. Struct. Mol. Biol. 21:927-936(2014).
RN [42]
RP SUMOYLATION [LARGE SCALE ANALYSIS] AT LYS-19, AND IDENTIFICATION BY MASS
RP SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=25772364; DOI=10.1016/j.celrep.2015.02.033;
RA Hendriks I.A., Treffers L.W., Verlaan-de Vries M., Olsen J.V.,
RA Vertegaal A.C.;
RT "SUMO-2 orchestrates chromatin modifiers in response to DNA damage.";
RL Cell Rep. 10:1778-1791(2015).
RN [43]
RP SUMOYLATION [LARGE SCALE ANALYSIS] AT LYS-19, AND IDENTIFICATION BY MASS
RP SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=25755297; DOI=10.1074/mcp.o114.044792;
RA Xiao Z., Chang J.G., Hendriks I.A., Sigurdsson J.O., Olsen J.V.,
RA Vertegaal A.C.;
RT "System-wide analysis of SUMOylation dynamics in response to replication
RT stress reveals novel small ubiquitin-like modified target proteins and
RT acceptor lysines relevant for genome stability.";
RL Mol. Cell. Proteomics 14:1419-1434(2015).
RN [44]
RP INTERACTION WITH NCBP3.
RX PubMed=26382858; DOI=10.1038/ncomms9192;
RA Gebhardt A., Habjan M., Benda C., Meiler A., Haas D.A., Hein M.Y., Mann A.,
RA Mann M., Habermann B., Pichlmair A.;
RT "mRNA export through an additional cap-binding complex consisting of NCBP1
RT and NCBP3.";
RL Nat. Commun. 6:8192-8192(2015).
RN [45]
RP SUMOYLATION [LARGE SCALE ANALYSIS] AT LYS-19; LYS-314 AND LYS-382, AND
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=28112733; DOI=10.1038/nsmb.3366;
RA Hendriks I.A., Lyon D., Young C., Jensen L.J., Vertegaal A.C.,
RA Nielsen M.L.;
RT "Site-specific mapping of the human SUMO proteome reveals co-modification
RT with phosphorylation.";
RL Nat. Struct. Mol. Biol. 24:325-336(2017).
RN [46]
RP INTERACTION WITH NRDE2.
RX PubMed=30538148; DOI=10.1261/rna.069773.118;
RA Jiao A.L., Perales R., Umbreit N.T., Haswell J.R., Piper M.E., Adams B.D.,
RA Pellman D., Kennedy S., Slack F.J.;
RT "Human nuclear RNAi-defective 2 (NRDE2) is an essential RNA splicing
RT factor.";
RL RNA 25:352-363(2019).
RN [47] {ECO:0007744|PDB:2J0Q, ECO:0007744|PDB:2J0S, ECO:0007744|PDB:2J0U}
RP X-RAY CRYSTALLOGRAPHY (2.21 ANGSTROMS) OF 2-411 IN THE EJC COMPLEX WITH
RP CASC3; MAGOH; RBM8A; ATP ANALOG AND POLY URACIL.
RX PubMed=16923391; DOI=10.1016/j.cell.2006.08.006;
RA Bono F., Ebert J., Lorentzen E., Conti E.;
RT "The crystal structure of the exon junction complex reveals how it
RT maintains a stable grip on mRNA.";
RL Cell 126:713-725(2006).
RN [48] {ECO:0007744|PDB:2HXY, ECO:0007744|PDB:2HYI}
RP X-RAY CRYSTALLOGRAPHY (2.3 ANGSTROMS) IN THE EJC COMPLEX WITH CASC3; MAGOH;
RP RBM8A; ATP ANALOG AND POLY URACIL.
RX PubMed=16931718; DOI=10.1126/science.1131981;
RA Andersen C.B., Ballut L., Johansen J.S., Chamieh H., Nielsen K.H.,
RA Oliveira C.L., Pedersen J.S., Seraphin B., Le Hir H., Andersen G.R.;
RT "Structure of the exon junction core complex with a trapped DEAD-box ATPase
RT bound to RNA.";
RL Science 313:1968-1972(2006).
RN [49]
RP X-RAY CRYSTALLOGRAPHY (2.3 ANGSTROMS) IN THE EJC COMPLEX WITH CASC3; MAGOH;
RP RBM8A; ATP ANALOG AND POLY URACIL.
RX PubMed=19033377; DOI=10.1261/rna.1283109;
RA Nielsen K.H., Chamieh H., Andersen C.B., Fredslund F., Hamborg K.,
RA Le Hir H., Andersen G.R.;
RT "Mechanism of ATP turnover inhibition in the EJC.";
RL RNA 15:67-75(2009).
RN [50] {ECO:0007744|PDB:2XB2}
RP X-RAY CRYSTALLOGRAPHY (3.40 ANGSTROMS) IN THE EJC COMPLEX WITH CASC3;
RP MAGOH; RBM8A; UPF3B; UPF2; RNA AND ATP ANALOG, AND IDENTIFICATION IN THE
RP EJC COMPLEX WITH UPF3A.
RX PubMed=20479275; DOI=10.1073/pnas.1000993107;
RA Buchwald G., Ebert J., Basquin C., Sauliere J., Jayachandran U., Bono F.,
RA Le Hir H., Conti E.;
RT "Insights into the recruitment of the NMD machinery from the crystal
RT structure of a core EJC-UPF3b complex.";
RL Proc. Natl. Acad. Sci. U.S.A. 107:10050-10055(2010).
RN [51] {ECO:0007744|PDB:4C9B}
RP X-RAY CRYSTALLOGRAPHY (2.00 ANGSTROMS) IN COMPLEX WITH CWC22, AND
RP MUTAGENESIS OF CYS-99 AND 300-ALA-ASN-301.
RX PubMed=24218557; DOI=10.1073/pnas.1314684110;
RA Buchwald G., Schussler S., Basquin C., Le Hir H., Conti E.;
RT "Crystal structure of the human eIF4AIII-CWC22 complex shows how a DEAD-box
RT protein is inhibited by a MIF4G domain.";
RL Proc. Natl. Acad. Sci. U.S.A. 110:E4611-E4618(2013).
RN [52] {ECO:0007744|PDB:5XJC}
RP STRUCTURE BY ELECTRON MICROSCOPY (3.60 ANGSTROMS), FUNCTION, SUBUNIT, AND
RP SUBCELLULAR LOCATION.
RX PubMed=28502770; DOI=10.1016/j.cell.2017.04.033;
RA Zhang X., Yan C., Hang J., Finci L.I., Lei J., Shi Y.;
RT "An Atomic Structure of the Human Spliceosome.";
RL Cell 169:918-929(2017).
RN [53] {ECO:0007744|PDB:5MQF}
RP STRUCTURE BY ELECTRON MICROSCOPY (5.90 ANGSTROMS), FUNCTION, SUBUNIT,
RP SUBCELLULAR LOCATION, AND IDENTIFICATION BY MASS SPECTROMETRY.
RX PubMed=28076346; DOI=10.1038/nature21079;
RA Bertram K., Agafonov D.E., Liu W.T., Dybkov O., Will C.L., Hartmuth K.,
RA Urlaub H., Kastner B., Stark H., Luhrmann R.;
RT "Cryo-EM structure of a human spliceosome activated for step 2 of
RT splicing.";
RL Nature 542:318-323(2017).
RN [54] {ECO:0007744|PDB:5YZG}
RP STRUCTURE BY ELECTRON MICROSCOPY (4.10 ANGSTROMS), FUNCTION, SUBUNIT, AND
RP SUBCELLULAR LOCATION.
RX PubMed=29301961; DOI=10.1126/science.aar6401;
RA Zhan X., Yan C., Zhang X., Lei J., Shi Y.;
RT "Structure of a human catalytic step I spliceosome.";
RL Science 359:537-545(2018).
CC -!- FUNCTION: ATP-dependent RNA helicase (PubMed:16170325). Involved in
CC pre-mRNA splicing as component of the spliceosome (PubMed:11991638,
CC PubMed:22961380, PubMed:28502770, PubMed:28076346, PubMed:29301961).
CC Core component of the splicing-dependent multiprotein exon junction
CC complex (EJC) deposited at splice junctions on mRNAs (PubMed:16209946,
CC PubMed:16170325, PubMed:16314458, PubMed:16923391, PubMed:16931718,
CC PubMed:19033377, PubMed:20479275). The EJC is a dynamic structure
CC consisting of core proteins and several peripheral nuclear and
CC cytoplasmic associated factors that join the complex only transiently
CC either during EJC assembly or during subsequent mRNA metabolism. The
CC EJC marks the position of the exon-exon junction in the mature mRNA for
CC the gene expression machinery and the core components remain bound to
CC spliced mRNAs throughout all stages of mRNA metabolism thereby
CC influencing downstream processes including nuclear mRNA export,
CC subcellular mRNA localization, translation efficiency and nonsense-
CC mediated mRNA decay (NMD). Its RNA-dependent ATPase and RNA-helicase
CC activities are induced by CASC3, but abolished in presence of the
CC MAGOH-RBM8A heterodimer, thereby trapping the ATP-bound EJC core onto
CC spliced mRNA in a stable conformation. The inhibition of ATPase
CC activity by the MAGOH-RBM8A heterodimer increases the RNA-binding
CC affinity of the EJC. Involved in translational enhancement of spliced
CC mRNAs after formation of the 80S ribosome complex. Binds spliced mRNA
CC in sequence-independent manner, 20-24 nucleotides upstream of mRNA
CC exon-exon junctions. Shows higher affinity for single-stranded RNA in
CC an ATP-bound core EJC complex than after the ATP is hydrolyzed.
CC Involved in the splicing modulation of BCL2L1/Bcl-X (and probably other
CC apoptotic genes); specifically inhibits formation of proapoptotic
CC isoforms such as Bcl-X(S); the function is different from the
CC established EJC assembly (PubMed:22203037). Involved in craniofacial
CC development (PubMed:24360810). {ECO:0000269|PubMed:11991638,
CC ECO:0000269|PubMed:15034551, ECO:0000269|PubMed:16170325,
CC ECO:0000269|PubMed:16209946, ECO:0000269|PubMed:16314458,
CC ECO:0000269|PubMed:16923391, ECO:0000269|PubMed:16931718,
CC ECO:0000269|PubMed:17375189, ECO:0000269|PubMed:19033377,
CC ECO:0000269|PubMed:19409878, ECO:0000269|PubMed:20479275,
CC ECO:0000269|PubMed:22203037, ECO:0000269|PubMed:22961380,
CC ECO:0000269|PubMed:24360810, ECO:0000269|PubMed:28076346,
CC ECO:0000269|PubMed:28502770, ECO:0000269|PubMed:29301961}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=ATP + H2O = ADP + H(+) + phosphate; Xref=Rhea:RHEA:13065,
CC ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:30616,
CC ChEBI:CHEBI:43474, ChEBI:CHEBI:456216; EC=3.6.4.13;
CC Evidence={ECO:0000269|PubMed:16170325, ECO:0000269|PubMed:17375189,
CC ECO:0000269|PubMed:22961380};
CC -!- ACTIVITY REGULATION: The ATPase activity is increased some 4-fold in
CC the presence of RNA. {ECO:0000269|PubMed:22961380}.
CC -!- SUBUNIT: Identified in the spliceosome C complex (PubMed:11991638,
CC PubMed:22961380, PubMed:28502770, PubMed:28076346, PubMed:29301961).
CC Core component of the mRNA splicing-dependent exon junction complex
CC (EJC); the core complex contains CASC3, EIF4A3, MAGOH or MAGOHB, and
CC RBM8A (PubMed:15034551, PubMed:14730019, PubMed:16170325,
CC PubMed:16314458, PubMed:23917022, PubMed:16923391, PubMed:16931718,
CC PubMed:19033377, PubMed:20479275). Interacts with CASC3, MAGOH, NXF1,
CC RBM8A and ALYREF/THOC4 (PubMed:14730019, PubMed:16170325,
CC PubMed:16495234, PubMed:22961380). May interact with NOM1. Interacts
CC with POLDIP3 (PubMed:18423201). Interacts with CWC22 and PRPF19 in an
CC RNA-independent manner (PubMed:22959432, PubMed:22961380,
CC PubMed:23236153, PubMed:24218557). Direct interaction with CWC22 is
CC mediated by the helicase C-terminal domain (PubMed:22959432,
CC PubMed:24218557). Full interaction with CWC22 occurs only when EIF4A3
CC is not part of the EJC and prevents EIF4A3 binding to RNA. Identified
CC in a complex composed of the EJC core, UPF3B and UPF2. The EJC core can
CC also interact with UPF3A (in vitro) (PubMed:20479275). Interacts with
CC NCBP3 (PubMed:26382858). Interacts with NRDE2 (PubMed:30538148).
CC Interacts with DHX34; the interaction is RNA-independent
CC (PubMed:25220460). {ECO:0000269|PubMed:11991638,
CC ECO:0000269|PubMed:14730019, ECO:0000269|PubMed:15034551,
CC ECO:0000269|PubMed:16170325, ECO:0000269|PubMed:16314458,
CC ECO:0000269|PubMed:16495234, ECO:0000269|PubMed:16923391,
CC ECO:0000269|PubMed:16931718, ECO:0000269|PubMed:18423201,
CC ECO:0000269|PubMed:19033377, ECO:0000269|PubMed:20479275,
CC ECO:0000269|PubMed:22959432, ECO:0000269|PubMed:22961380,
CC ECO:0000269|PubMed:23236153, ECO:0000269|PubMed:23917022,
CC ECO:0000269|PubMed:24218557, ECO:0000269|PubMed:25220460,
CC ECO:0000269|PubMed:26382858, ECO:0000269|PubMed:28076346,
CC ECO:0000269|PubMed:28502770, ECO:0000269|PubMed:29301961,
CC ECO:0000269|PubMed:30538148}.
CC -!- INTERACTION:
CC P38919; Q9H257-2: CARD9; NbExp=3; IntAct=EBI-299104, EBI-11530605;
CC P38919; O15234: CASC3; NbExp=33; IntAct=EBI-299104, EBI-299118;
CC P38919; Q6PII3: CCDC174; NbExp=4; IntAct=EBI-299104, EBI-747830;
CC P38919; Q96GN5: CDCA7L; NbExp=3; IntAct=EBI-299104, EBI-5278764;
CC P38919; Q6P9H4: CNKSR3; NbExp=3; IntAct=EBI-299104, EBI-10253274;
CC P38919; Q9HCG8: CWC22; NbExp=6; IntAct=EBI-299104, EBI-373289;
CC P38919; Q96D03: DDIT4L; NbExp=3; IntAct=EBI-299104, EBI-742054;
CC P38919; Q9NY93: DDX56; NbExp=3; IntAct=EBI-299104, EBI-372376;
CC P38919; Q9NRI5-2: DISC1; NbExp=3; IntAct=EBI-299104, EBI-11988027;
CC P38919; P55039: DRG2; NbExp=3; IntAct=EBI-299104, EBI-750565;
CC P38919; Q96KQ7: EHMT2; NbExp=3; IntAct=EBI-299104, EBI-744366;
CC P38919; Q8TBB1: LNX1; NbExp=3; IntAct=EBI-299104, EBI-739832;
CC P38919; P61326: MAGOH; NbExp=30; IntAct=EBI-299104, EBI-299134;
CC P38919; P50221: MEOX1; NbExp=3; IntAct=EBI-299104, EBI-2864512;
CC P38919; Q6FHY5: MEOX2; NbExp=3; IntAct=EBI-299104, EBI-16439278;
CC P38919; Q9GZT8: NIF3L1; NbExp=3; IntAct=EBI-299104, EBI-740897;
CC P38919; Q5C9Z4: NOM1; NbExp=3; IntAct=EBI-299104, EBI-2685618;
CC P38919; Q3KNR5: PAX4; NbExp=3; IntAct=EBI-299104, EBI-10240813;
CC P38919; Q53EL6: PDCD4; NbExp=6; IntAct=EBI-299104, EBI-935824;
CC P38919; Q9NRD5: PICK1; NbExp=3; IntAct=EBI-299104, EBI-79165;
CC P38919; P62487: POLR2G; NbExp=3; IntAct=EBI-299104, EBI-347928;
CC P38919; O14744: PRMT5; NbExp=3; IntAct=EBI-299104, EBI-351098;
CC P38919; P25786: PSMA1; NbExp=3; IntAct=EBI-299104, EBI-359352;
CC P38919; Q9Y5S9: RBM8A; NbExp=21; IntAct=EBI-299104, EBI-447231;
CC P38919; Q04864-2: REL; NbExp=3; IntAct=EBI-299104, EBI-10829018;
CC P38919; Q9Y2W1: THRAP3; NbExp=2; IntAct=EBI-299104, EBI-352039;
CC P38919; P14373: TRIM27; NbExp=3; IntAct=EBI-299104, EBI-719493;
CC P38919; Q9BZI7: UPF3B; NbExp=9; IntAct=EBI-299104, EBI-372780;
CC P38919; Q9H8Y1: VRTN; NbExp=3; IntAct=EBI-299104, EBI-12894399;
CC P38919; P98169: ZXDB; NbExp=3; IntAct=EBI-299104, EBI-17493569;
CC -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000269|PubMed:10623621,
CC ECO:0000269|PubMed:11991638, ECO:0000269|PubMed:22961380,
CC ECO:0000269|PubMed:28076346, ECO:0000269|PubMed:28502770,
CC ECO:0000269|PubMed:29301961}. Nucleus speckle
CC {ECO:0000269|PubMed:10623621}. Cytoplasm
CC {ECO:0000250|UniProtKB:Q3B8Q2}. Note=Nucleocytoplasmic shuttling
CC protein. Travels to the cytoplasm as part of the exon junction complex
CC (EJC) bound to mRNA. Detected in dendritic layer as well as the nuclear
CC and cytoplasmic (somatic) compartments of neurons. Colocalizes with
CC STAU1 and FMR1 in dendrites (By similarity).
CC {ECO:0000250|UniProtKB:Q3B8Q2}.
CC -!- TISSUE SPECIFICITY: Ubiquitously expressed.
CC {ECO:0000269|PubMed:10623621}.
CC -!- DISEASE: Richieri-Costa-Pereira syndrome (RCPS) [MIM:268305]: A
CC syndrome characterized by a unique pattern of anomalies consisting of
CC microstomia, micrognathia, abnormal fusion of mandible, cleft
CC palate/Robin sequence, absence of central lower incisors, minor ears
CC anomalies, hypoplastic first ray, abnormal tibiae, hypoplastic
CC halluces, and clubfeet. Learning disability is also a common finding.
CC {ECO:0000269|PubMed:24360810}. Note=The disease is caused by variants
CC affecting the gene represented in this entry. EIF4A3 mutations
CC resulting in Richieri-Costa-Pereira syndrome include a repeat expansion
CC of 18 or 20 nucleotides in the 5' untranslated region. Affected
CC individuals have 14 to 16 repeats, while healthy individuals have 3 to
CC 12 repeats (PubMed:24360810). {ECO:0000269|PubMed:24360810}.
CC -!- SIMILARITY: Belongs to the DEAD box helicase family. eIF4A subfamily.
CC {ECO:0000305}.
CC -!- SEQUENCE CAUTION:
CC Sequence=BAA04879.2; Type=Erroneous initiation; Note=Extended N-terminus.; Evidence={ECO:0000305};
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DR EMBL; X79538; CAA56074.1; -; mRNA.
DR EMBL; D21853; BAA04879.2; ALT_INIT; mRNA.
DR EMBL; AK290608; BAF83297.1; -; mRNA.
DR EMBL; CR456750; CAG33031.1; -; mRNA.
DR EMBL; AC087741; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; CH471099; EAW89584.1; -; Genomic_DNA.
DR EMBL; BC003662; AAH03662.1; -; mRNA.
DR EMBL; BC004386; AAH04386.1; -; mRNA.
DR EMBL; BC011151; AAH11151.1; -; mRNA.
DR CCDS; CCDS11767.1; -.
DR PIR; S45142; S45142.
DR RefSeq; NP_055555.1; NM_014740.3.
DR PDB; 2HXY; X-ray; 3.30 A; A/B/C/D=23-411.
DR PDB; 2HYI; X-ray; 2.30 A; C/I=1-411.
DR PDB; 2J0Q; X-ray; 3.20 A; A/B=2-411.
DR PDB; 2J0S; X-ray; 2.21 A; A=2-411.
DR PDB; 2J0U; X-ray; 3.00 A; A/B=38-411.
DR PDB; 2XB2; X-ray; 3.40 A; A/X=1-411.
DR PDB; 3EX7; X-ray; 2.30 A; C/H=1-411.
DR PDB; 4C9B; X-ray; 2.00 A; A=1-411.
DR PDB; 5MQF; EM; 5.90 A; p=1-411.
DR PDB; 5XJC; EM; 3.60 A; u=1-411.
DR PDB; 5YZG; EM; 4.10 A; u=1-411.
DR PDB; 6ICZ; EM; 3.00 A; u=1-411.
DR PDB; 6QDV; EM; 3.30 A; 7=22-404.
DR PDB; 6YVH; X-ray; 3.19 A; H/J/K/L=246-411.
DR PDB; 7A5P; EM; 5.00 A; y=1-411.
DR PDBsum; 2HXY; -.
DR PDBsum; 2HYI; -.
DR PDBsum; 2J0Q; -.
DR PDBsum; 2J0S; -.
DR PDBsum; 2J0U; -.
DR PDBsum; 2XB2; -.
DR PDBsum; 3EX7; -.
DR PDBsum; 4C9B; -.
DR PDBsum; 5MQF; -.
DR PDBsum; 5XJC; -.
DR PDBsum; 5YZG; -.
DR PDBsum; 6ICZ; -.
DR PDBsum; 6QDV; -.
DR PDBsum; 6YVH; -.
DR PDBsum; 7A5P; -.
DR AlphaFoldDB; P38919; -.
DR SMR; P38919; -.
DR BioGRID; 115119; 445.
DR ComplexPortal; CPX-1941; Exon junction core complex, MAGOH variant.
DR ComplexPortal; CPX-682; Exon junction core complex, MAGOHB variant.
DR CORUM; P38919; -.
DR DIP; DIP-33218N; -.
DR IntAct; P38919; 209.
DR MINT; P38919; -.
DR STRING; 9606.ENSP00000269349; -.
DR BindingDB; P38919; -.
DR ChEMBL; CHEMBL4105832; -.
DR TCDB; 3.A.18.1.1; the nuclear mrna exporter (mrna-e) family.
DR GlyGen; P38919; 2 sites, 1 O-linked glycan (2 sites).
DR iPTMnet; P38919; -.
DR PhosphoSitePlus; P38919; -.
DR SwissPalm; P38919; -.
DR BioMuta; EIF4A3; -.
DR DMDM; 20532400; -.
DR REPRODUCTION-2DPAGE; IPI00009328; -.
DR EPD; P38919; -.
DR jPOST; P38919; -.
DR MassIVE; P38919; -.
DR MaxQB; P38919; -.
DR PaxDb; P38919; -.
DR PeptideAtlas; P38919; -.
DR PRIDE; P38919; -.
DR ProteomicsDB; 55305; -.
DR Antibodypedia; 19760; 255 antibodies from 31 providers.
DR DNASU; 9775; -.
DR Ensembl; ENST00000647795.1; ENSP00000497661.1; ENSG00000141543.12.
DR Ensembl; ENST00000649764.2; ENSP00000497641.1; ENSG00000141543.12.
DR GeneID; 9775; -.
DR KEGG; hsa:9775; -.
DR MANE-Select; ENST00000649764.2; ENSP00000497641.1; NM_014740.4; NP_055555.1.
DR UCSC; uc002jxs.3; human.
DR CTD; 9775; -.
DR DisGeNET; 9775; -.
DR GeneCards; EIF4A3; -.
DR HGNC; HGNC:18683; EIF4A3.
DR HPA; ENSG00000141543; Low tissue specificity.
DR MalaCards; EIF4A3; -.
DR MIM; 268305; phenotype.
DR MIM; 608546; gene.
DR neXtProt; NX_P38919; -.
DR OpenTargets; ENSG00000141543; -.
DR Orphanet; 3102; Richieri Costa-Pereira syndrome.
DR PharmGKB; PA162384945; -.
DR VEuPathDB; HostDB:ENSG00000141543; -.
DR eggNOG; KOG0328; Eukaryota.
DR GeneTree; ENSGT00940000155037; -.
DR HOGENOM; CLU_003041_1_0_1; -.
DR InParanoid; P38919; -.
DR OMA; FGCQALV; -.
DR OrthoDB; 726081at2759; -.
DR PhylomeDB; P38919; -.
DR TreeFam; TF300466; -.
DR BRENDA; 3.6.4.13; 2681.
DR PathwayCommons; P38919; -.
DR Reactome; R-HSA-1169408; ISG15 antiviral mechanism.
DR Reactome; R-HSA-159236; Transport of Mature mRNA derived from an Intron-Containing Transcript.
DR Reactome; R-HSA-429947; Deadenylation of mRNA.
DR Reactome; R-HSA-72163; mRNA Splicing - Major Pathway.
DR Reactome; R-HSA-72187; mRNA 3'-end processing.
DR Reactome; R-HSA-73856; RNA Polymerase II Transcription Termination.
DR Reactome; R-HSA-9010553; Regulation of expression of SLITs and ROBOs.
DR Reactome; R-HSA-975957; Nonsense Mediated Decay (NMD) enhanced by the Exon Junction Complex (EJC).
DR SignaLink; P38919; -.
DR SIGNOR; P38919; -.
DR BioGRID-ORCS; 9775; 809 hits in 1054 CRISPR screens.
DR ChiTaRS; EIF4A3; human.
DR EvolutionaryTrace; P38919; -.
DR GeneWiki; EIF4A3; -.
DR GenomeRNAi; 9775; -.
DR Pharos; P38919; Tchem.
DR PRO; PR:P38919; -.
DR Proteomes; UP000005640; Chromosome 17.
DR RNAct; P38919; protein.
DR Bgee; ENSG00000141543; Expressed in type B pancreatic cell and 208 other tissues.
DR ExpressionAtlas; P38919; baseline and differential.
DR Genevisible; P38919; HS.
DR GO; GO:0071013; C:catalytic step 2 spliceosome; IDA:UniProtKB.
DR GO; GO:0005737; C:cytoplasm; IDA:HGNC-UCL.
DR GO; GO:0005829; C:cytosol; TAS:Reactome.
DR GO; GO:0030425; C:dendrite; IEA:Ensembl.
DR GO; GO:0035145; C:exon-exon junction complex; IDA:UniProtKB.
DR GO; GO:0098978; C:glutamatergic synapse; IEA:Ensembl.
DR GO; GO:0016020; C:membrane; HDA:UniProtKB.
DR GO; GO:0043025; C:neuronal cell body; IEA:Ensembl.
DR GO; GO:0016607; C:nuclear speck; IEA:UniProtKB-SubCell.
DR GO; GO:0005730; C:nucleolus; IBA:GO_Central.
DR GO; GO:0005654; C:nucleoplasm; IDA:HPA.
DR GO; GO:0005634; C:nucleus; IDA:UniProtKB.
DR GO; GO:0099524; C:postsynaptic cytosol; IEA:Ensembl.
DR GO; GO:0071006; C:U2-type catalytic step 1 spliceosome; IDA:UniProtKB.
DR GO; GO:0005524; F:ATP binding; IDA:HGNC-UCL.
DR GO; GO:0016887; F:ATP hydrolysis activity; IEA:RHEA.
DR GO; GO:0003729; F:mRNA binding; IDA:UniProtKB.
DR GO; GO:0008143; F:poly(A) binding; IDA:HGNC-UCL.
DR GO; GO:0043021; F:ribonucleoprotein complex binding; IEA:Ensembl.
DR GO; GO:0003723; F:RNA binding; HDA:UniProtKB.
DR GO; GO:0003724; F:RNA helicase activity; IDA:HGNC-UCL.
DR GO; GO:0035613; F:RNA stem-loop binding; IEA:Ensembl.
DR GO; GO:0035368; F:selenocysteine insertion sequence binding; IEA:Ensembl.
DR GO; GO:0045182; F:translation regulator activity; IEA:Ensembl.
DR GO; GO:0008306; P:associative learning; IEA:Ensembl.
DR GO; GO:1990416; P:cellular response to brain-derived neurotrophic factor stimulus; IEA:Ensembl.
DR GO; GO:0072715; P:cellular response to selenite ion; IEA:Ensembl.
DR GO; GO:0048701; P:embryonic cranial skeleton morphogenesis; IMP:UniProtKB.
DR GO; GO:0035640; P:exploration behavior; IEA:Ensembl.
DR GO; GO:0006406; P:mRNA export from nucleus; IC:ComplexPortal.
DR GO; GO:0000398; P:mRNA splicing, via spliceosome; IDA:UniProtKB.
DR GO; GO:0090394; P:negative regulation of excitatory postsynaptic potential; IEA:Ensembl.
DR GO; GO:1904570; P:negative regulation of selenocysteine incorporation; IEA:Ensembl.
DR GO; GO:1904574; P:negative regulation of selenocysteine insertion sequence binding; IEA:Ensembl.
DR GO; GO:0017148; P:negative regulation of translation; IDA:HGNC-UCL.
DR GO; GO:0000184; P:nuclear-transcribed mRNA catabolic process, nonsense-mediated decay; IMP:UniProtKB.
DR GO; GO:0045727; P:positive regulation of translation; IMP:UniProtKB.
DR GO; GO:2000622; P:regulation of nuclear-transcribed mRNA catabolic process, nonsense-mediated decay; IDA:ComplexPortal.
DR GO; GO:0099578; P:regulation of translation at postsynapse, modulating synaptic transmission; IEA:Ensembl.
DR GO; GO:0014070; P:response to organic cyclic compound; IEA:Ensembl.
DR GO; GO:0006364; P:rRNA processing; IEA:UniProtKB-KW.
DR DisProt; DP02069; -.
DR Gene3D; 3.40.50.300; -; 2.
DR IDEAL; IID00370; -.
DR InterPro; IPR011545; DEAD/DEAH_box_helicase_dom.
DR InterPro; IPR014001; Helicase_ATP-bd.
DR InterPro; IPR001650; Helicase_C.
DR InterPro; IPR027417; P-loop_NTPase.
DR InterPro; IPR000629; RNA-helicase_DEAD-box_CS.
DR InterPro; IPR014014; RNA_helicase_DEAD_Q_motif.
DR Pfam; PF00270; DEAD; 1.
DR Pfam; PF00271; Helicase_C; 1.
DR SMART; SM00487; DEXDc; 1.
DR SMART; SM00490; HELICc; 1.
DR SUPFAM; SSF52540; SSF52540; 1.
DR PROSITE; PS00039; DEAD_ATP_HELICASE; 1.
DR PROSITE; PS51192; HELICASE_ATP_BIND_1; 1.
DR PROSITE; PS51194; HELICASE_CTER; 1.
DR PROSITE; PS51195; Q_MOTIF; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Acetylation; ATP-binding; Cytoplasm;
KW Direct protein sequencing; Disease variant; Helicase; Hydrolase;
KW Isopeptide bond; mRNA processing; mRNA splicing; mRNA transport;
KW Nonsense-mediated mRNA decay; Nucleotide-binding; Nucleus; Phosphoprotein;
KW Reference proteome; RNA-binding; rRNA processing; Spliceosome;
KW Translation regulation; Transport; Ubl conjugation.
FT CHAIN 1..411
FT /note="Eukaryotic initiation factor 4A-III"
FT /id="PRO_0000423267"
FT INIT_MET 1
FT /note="Removed; alternate"
FT /evidence="ECO:0000269|Ref.8, ECO:0007744|PubMed:19369195,
FT ECO:0007744|PubMed:19413330, ECO:0007744|PubMed:20068231,
FT ECO:0007744|PubMed:21406692, ECO:0007744|PubMed:22223895,
FT ECO:0007744|PubMed:22814378"
FT CHAIN 2..411
FT /note="Eukaryotic initiation factor 4A-III, N-terminally
FT processed"
FT /id="PRO_0000054942"
FT DOMAIN 69..239
FT /note="Helicase ATP-binding"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00541"
FT DOMAIN 250..411
FT /note="Helicase C-terminal"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00542"
FT MOTIF 38..66
FT /note="Q motif"
FT MOTIF 187..190
FT /note="DEAD box"
FT /evidence="ECO:0000305"
FT BINDING 60
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000269|PubMed:16923391,
FT ECO:0000269|PubMed:16931718, ECO:0000269|PubMed:19033377,
FT ECO:0000269|PubMed:20479275, ECO:0007744|PDB:2HYI,
FT ECO:0007744|PDB:2J0Q, ECO:0007744|PDB:2J0S,
FT ECO:0007744|PDB:2XB2, ECO:0007744|PDB:3EX7"
FT BINDING 65
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000269|PubMed:16923391,
FT ECO:0000269|PubMed:16931718, ECO:0000269|PubMed:19033377,
FT ECO:0000269|PubMed:20479275, ECO:0007744|PDB:2HYI,
FT ECO:0007744|PDB:2J0Q, ECO:0007744|PDB:2J0S,
FT ECO:0007744|PDB:2XB2, ECO:0007744|PDB:3EX7"
FT BINDING 85..90
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000269|PubMed:16923391,
FT ECO:0000269|PubMed:16931718, ECO:0000269|PubMed:19033377,
FT ECO:0000269|PubMed:20479275, ECO:0007744|PDB:2HYI,
FT ECO:0007744|PDB:2J0Q, ECO:0007744|PDB:2J0S,
FT ECO:0007744|PDB:2XB2, ECO:0007744|PDB:3EX7"
FT BINDING 342
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000269|PubMed:16923391,
FT ECO:0000269|PubMed:16931718, ECO:0000269|PubMed:19033377,
FT ECO:0000269|PubMed:20479275, ECO:0007744|PDB:2HYI,
FT ECO:0007744|PDB:2J0Q, ECO:0007744|PDB:2J0S,
FT ECO:0007744|PDB:2XB2, ECO:0007744|PDB:3EX7"
FT BINDING 367..371
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000269|PubMed:16923391,
FT ECO:0000269|PubMed:16931718, ECO:0000269|PubMed:19033377,
FT ECO:0000269|PubMed:20479275, ECO:0007744|PDB:2HYI,
FT ECO:0007744|PDB:2J0Q, ECO:0007744|PDB:2J0S,
FT ECO:0007744|PDB:2XB2, ECO:0007744|PDB:3EX7"
FT MOD_RES 1
FT /note="N-acetylmethionine"
FT /evidence="ECO:0007744|PubMed:20068231,
FT ECO:0007744|PubMed:21406692"
FT MOD_RES 2
FT /note="N-acetylalanine; in Eukaryotic initiation factor 4A-
FT III, N-terminally processed"
FT /evidence="ECO:0000269|Ref.8, ECO:0007744|PubMed:19369195,
FT ECO:0007744|PubMed:19413330, ECO:0007744|PubMed:20068231,
FT ECO:0007744|PubMed:21406692, ECO:0007744|PubMed:22223895,
FT ECO:0007744|PubMed:22814378"
FT MOD_RES 10
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:P60842"
FT MOD_RES 12
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:20068231,
FT ECO:0007744|PubMed:21406692, ECO:0007744|PubMed:23186163"
FT MOD_RES 124
FT /note="N6-acetyllysine"
FT /evidence="ECO:0000250|UniProtKB:P60842"
FT MOD_RES 163
FT /note="Phosphothreonine"
FT /evidence="ECO:0007744|PubMed:18669648,
FT ECO:0007744|PubMed:20068231, ECO:0007744|PubMed:23186163"
FT MOD_RES 198
FT /note="N6-acetyllysine"
FT /evidence="ECO:0000250|UniProtKB:P60843"
FT MOD_RES 296
FT /note="N6-acetyllysine"
FT /evidence="ECO:0007744|PubMed:19608861"
FT MOD_RES 321
FT /note="N6-acetyllysine"
FT /evidence="ECO:0007744|PubMed:19608861"
FT CROSSLNK 19
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2)"
FT /evidence="ECO:0007744|PubMed:25218447,
FT ECO:0007744|PubMed:25755297, ECO:0007744|PubMed:25772364,
FT ECO:0007744|PubMed:28112733"
FT CROSSLNK 152
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2)"
FT /evidence="ECO:0000250|UniProtKB:P60842"
FT CROSSLNK 314
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2)"
FT /evidence="ECO:0007744|PubMed:28112733"
FT CROSSLNK 374
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2)"
FT /evidence="ECO:0000250|UniProtKB:P60842"
FT CROSSLNK 382
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2)"
FT /evidence="ECO:0007744|PubMed:28112733"
FT VARIANT 270
FT /note="D -> G (in RCPS; dbSNP:rs587777204)"
FT /evidence="ECO:0000269|PubMed:24360810"
FT /id="VAR_071090"
FT MUTAGEN 88
FT /note="K->A: ATPase activity is not increased by the
FT presence of CASC3. Does not prevent EJC formation. Prevents
FT the EJC disassembly."
FT /evidence="ECO:0000269|PubMed:16170325"
FT MUTAGEN 99
FT /note="C->Q: No effect on interaction with CWC22."
FT /evidence="ECO:0000269|PubMed:24218557"
FT MUTAGEN 270
FT /note="D->K: Loss of CWC22-binding and loss of
FT incorporation into EJCs; when associated with K-273."
FT /evidence="ECO:0000269|PubMed:22959432"
FT MUTAGEN 273
FT /note="D->K: Loss of CWC22-binding and loss of
FT incorporation into EJCs; when associated with K-270."
FT /evidence="ECO:0000269|PubMed:22959432"
FT MUTAGEN 276..277
FT /note="TI->GD: Loss of CWC22-binding and loss of
FT incorporation into EJCs."
FT /evidence="ECO:0000269|PubMed:22959432"
FT MUTAGEN 300..301
FT /note="AN->RD: Decreased interaction with CWC22."
FT /evidence="ECO:0000269|PubMed:24218557"
FT MUTAGEN 301..303
FT /note="NFT->LAG: Loss of CWC22-binding and loss of
FT incorporation into EJCs."
FT /evidence="ECO:0000269|PubMed:22959432"
FT MUTAGEN 334
FT /note="T->V: Reduced incorporation into EJCs."
FT /evidence="ECO:0000269|PubMed:23236153"
FT MUTAGEN 401
FT /note="D->K: Loss of incorporation into EJCs; when
FT associated with R-402."
FT /evidence="ECO:0000269|PubMed:22961380"
FT MUTAGEN 402
FT /note="E->R: Loss of incorporation into EJCs; when
FT associated with K-401."
FT /evidence="ECO:0000269|PubMed:22961380"
FT CONFLICT 210
FT /note="P -> S (in Ref. 1; CAA56074)"
FT /evidence="ECO:0000305"
FT CONFLICT 370
FT /note="R -> Q (in Ref. 1; CAA56074)"
FT /evidence="ECO:0000305"
FT HELIX 23..25
FT /evidence="ECO:0007829|PDB:4C9B"
FT STRAND 28..32
FT /evidence="ECO:0007829|PDB:4C9B"
FT HELIX 40..42
FT /evidence="ECO:0007829|PDB:4C9B"
FT HELIX 47..56
FT /evidence="ECO:0007829|PDB:4C9B"
FT HELIX 65..73
FT /evidence="ECO:0007829|PDB:4C9B"
FT STRAND 78..81
FT /evidence="ECO:0007829|PDB:4C9B"
FT STRAND 84..86
FT /evidence="ECO:0007829|PDB:2HXY"
FT HELIX 88..98
FT /evidence="ECO:0007829|PDB:4C9B"
FT STRAND 102..104
FT /evidence="ECO:0007829|PDB:2J0U"
FT STRAND 109..112
FT /evidence="ECO:0007829|PDB:4C9B"
FT HELIX 116..129
FT /evidence="ECO:0007829|PDB:4C9B"
FT TURN 130..134
FT /evidence="ECO:0007829|PDB:4C9B"
FT STRAND 137..139
FT /evidence="ECO:0007829|PDB:4C9B"
FT HELIX 143..145
FT /evidence="ECO:0007829|PDB:4C9B"
FT HELIX 146..155
FT /evidence="ECO:0007829|PDB:4C9B"
FT STRAND 158..162
FT /evidence="ECO:0007829|PDB:4C9B"
FT HELIX 164..172
FT /evidence="ECO:0007829|PDB:4C9B"
FT STRAND 183..186
FT /evidence="ECO:0007829|PDB:4C9B"
FT HELIX 189..195
FT /evidence="ECO:0007829|PDB:4C9B"
FT HELIX 198..206
FT /evidence="ECO:0007829|PDB:4C9B"
FT STRAND 213..219
FT /evidence="ECO:0007829|PDB:4C9B"
FT HELIX 223..232
FT /evidence="ECO:0007829|PDB:4C9B"
FT STRAND 237..241
FT /evidence="ECO:0007829|PDB:4C9B"
FT HELIX 243..245
FT /evidence="ECO:0007829|PDB:2J0S"
FT STRAND 251..260
FT /evidence="ECO:0007829|PDB:4C9B"
FT HELIX 261..263
FT /evidence="ECO:0007829|PDB:4C9B"
FT HELIX 264..274
FT /evidence="ECO:0007829|PDB:4C9B"
FT STRAND 278..283
FT /evidence="ECO:0007829|PDB:4C9B"
FT HELIX 287..299
FT /evidence="ECO:0007829|PDB:4C9B"
FT STRAND 304..307
FT /evidence="ECO:0007829|PDB:4C9B"
FT STRAND 309..311
FT /evidence="ECO:0007829|PDB:2J0U"
FT HELIX 313..324
FT /evidence="ECO:0007829|PDB:4C9B"
FT STRAND 329..333
FT /evidence="ECO:0007829|PDB:4C9B"
FT HELIX 335..337
FT /evidence="ECO:0007829|PDB:2J0S"
FT STRAND 338..340
FT /evidence="ECO:0007829|PDB:2J0S"
FT STRAND 346..353
FT /evidence="ECO:0007829|PDB:4C9B"
FT STRAND 356..358
FT /evidence="ECO:0007829|PDB:4C9B"
FT HELIX 360..365
FT /evidence="ECO:0007829|PDB:4C9B"
FT STRAND 367..369
FT /evidence="ECO:0007829|PDB:4C9B"
FT HELIX 370..372
FT /evidence="ECO:0007829|PDB:2J0S"
FT STRAND 375..382
FT /evidence="ECO:0007829|PDB:4C9B"
FT HELIX 383..385
FT /evidence="ECO:0007829|PDB:4C9B"
FT HELIX 386..396
FT /evidence="ECO:0007829|PDB:4C9B"
FT STRAND 400..402
FT /evidence="ECO:0007829|PDB:2HYI"
FT HELIX 405..410
FT /evidence="ECO:0007829|PDB:4C9B"
SQ SEQUENCE 411 AA; 46871 MW; 3A21888CA96CA5EA CRC64;
MATTATMATS GSARKRLLKE EDMTKVEFET SEEVDVTPTF DTMGLREDLL RGIYAYGFEK
PSAIQQRAIK QIIKGRDVIA QSQSGTGKTA TFSISVLQCL DIQVRETQAL ILAPTRELAV
QIQKGLLALG DYMNVQCHAC IGGTNVGEDI RKLDYGQHVV AGTPGRVFDM IRRRSLRTRA
IKMLVLDEAD EMLNKGFKEQ IYDVYRYLPP ATQVVLISAT LPHEILEMTN KFMTDPIRIL
VKRDELTLEG IKQFFVAVER EEWKFDTLCD LYDTLTITQA VIFCNTKRKV DWLTEKMREA
NFTVSSMHGD MPQKERESIM KEFRSGASRV LISTDVWARG LDVPQVSLII NYDLPNNREL
YIHRIGRSGR YGRKGVAINF VKNDDIRILR DIEQYYSTQI DEMPMNVADL I
