EIF3E_HUMAN
ID EIF3E_HUMAN Reviewed; 445 AA.
AC P60228; O43902; Q64058; Q64059; Q64252; Q6FG33; Q8WVK4;
DT 16-JAN-2004, integrated into UniProtKB/Swiss-Prot.
DT 16-JAN-2004, sequence version 1.
DT 03-AUG-2022, entry version 191.
DE RecName: Full=Eukaryotic translation initiation factor 3 subunit E {ECO:0000255|HAMAP-Rule:MF_03004};
DE Short=eIF3e {ECO:0000255|HAMAP-Rule:MF_03004};
DE AltName: Full=Eukaryotic translation initiation factor 3 subunit 6 {ECO:0000255|HAMAP-Rule:MF_03004};
DE AltName: Full=Viral integration site protein INT-6 homolog;
DE AltName: Full=eIF-3 p48 {ECO:0000255|HAMAP-Rule:MF_03004};
GN Name=EIF3E {ECO:0000255|HAMAP-Rule:MF_03004};
GN Synonyms=EIF3S6 {ECO:0000255|HAMAP-Rule:MF_03004},
GN INT6 {ECO:0000255|HAMAP-Rule:MF_03004};
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], PROTEIN SEQUENCE OF 280-289 AND 427-436,
RP INTERACTION WITH EIF3A, IDENTIFICATION IN THE EIF-3 COMPLEX, AND TISSUE
RP SPECIFICITY.
RC TISSUE=Liver;
RX PubMed=9295280; DOI=10.1074/jbc.272.38.23477;
RA Asano K., Merrick W.C., Hershey J.W.B.;
RT "The translation initiation factor eIF3-p48 subunit is encoded by int-6, a
RT site of frequent integration by the mouse mammary tumor virus genome.";
RL J. Biol. Chem. 272:23477-23480(1997).
RN [2]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA / MRNA].
RC TISSUE=Lung;
RX PubMed=9403073; DOI=10.1006/geno.1997.4996;
RA Miyazaki S., Imatani A., Ballard L., Marchetti A., Buttitta F.,
RA Albertsen H., Nevanlinna H.A., Gallahan D., Callahan R.;
RT "The chromosome location of the human homolog of the mouse mammary tumor-
RT associated gene INT6 and its status in human breast carcinomas.";
RL Genomics 46:155-158(1997).
RN [3]
RP NUCLEOTIDE SEQUENCE [MRNA], INTERACTION WITH TAX-1, SUBCELLULAR LOCATION,
RP AND TISSUE SPECIFICITY.
RX PubMed=8688078; DOI=10.1126/science.273.5277.951;
RA Desbois C., Rousset R., Bantignies F., Jalinot P.;
RT "Exclusion of Int-6 from PML nuclear bodies by binding to the HTLV-I Tax
RT oncoprotein.";
RL Science 273:951-953(1996).
RN [4]
RP NUCLEOTIDE SEQUENCE [MRNA], INTERACTION WITH TAX-1, AND SUBCELLULAR
RP LOCATION.
RX PubMed=12386384; DOI=10.1007/bf02253422;
RA Neuvert C., Jin D.-Y., Semmes O.J., Diella F., Callahan R., Jeang K.-T.;
RT "Divergent subcellular locations of HTLV-I Tax and Int-6: a contrast
RT between in vitro protein-protein binding and intracellular protein
RT colocalization.";
RL J. Biomed. Sci. 4:229-234(1997).
RN [5]
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 [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], AND VARIANT VAL-185.
RC TISSUE=Bone marrow, Brain, Lung, and Muscle;
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 2-9; 60-71; 164-172; 256-265 AND 370-376, CLEAVAGE OF
RP INITIATOR METHIONINE, ACETYLATION AT ALA-2, AND IDENTIFICATION BY MASS
RP SPECTROMETRY.
RC TISSUE=Colon carcinoma, and Mammary carcinoma;
RA Bienvenut W.V., Heiserich L., Gottlieb E., Matallanas D., Cooper W.N.,
RA Kolch W.;
RL Submitted (MAR-2008) to UniProtKB.
RN [9]
RP INTERACTION WITH EIF3C AND TRIM27, AND SUBCELLULAR LOCATION.
RX PubMed=10504338; DOI=10.1242/jcs.112.19.3331;
RA Morris-Desbois C., Bochard V., Reynaud C., Jalinot P.;
RT "Interaction between the Ret finger protein and the Int-6 gene product and
RT co-localisation into nuclear bodies.";
RL J. Cell Sci. 112:3331-3342(1999).
RN [10]
RP INTERACTION WITH EIF3B.
RX PubMed=11457827; DOI=10.1074/jbc.m102161200;
RA Shalev A., Valasek L., Pise-Masison C.A., Radonovich M., Phan L.,
RA Clayton J., He H., Brady J.N., Hinnebusch A.G., Asano K.;
RT "Saccharomyces cerevisiae protein Pci8p and human protein eIF3e/Int-6
RT interact with the eIF3 core complex by binding to cognate eIF3b subunits.";
RL J. Biol. Chem. 276:34948-34957(2001).
RN [11]
RP INTERACTION WITH EIF3L.
RX PubMed=11590142; DOI=10.1074/jbc.m104966200;
RA Morris-Desbois C., Rety S., Ferro M., Garin J., Jalinot P.;
RT "The human protein HSPC021 interacts with Int-6 and is associated with
RT eukaryotic translation initiation factor 3.";
RL J. Biol. Chem. 276:45988-45995(2001).
RN [12]
RP INTERACTION WITH COPS3; COPS6; COPS7 AND PSMC6.
RX PubMed=12220626; DOI=10.1016/s0014-5793(02)03147-2;
RA Hoareau Alves K., Bochard V., Rety S., Jalinot P.;
RT "Association of the mammalian proto-oncoprotein Int-6 with the three
RT protein complexes eIF3, COP9 signalosome and 26S proteasome.";
RL FEBS Lett. 527:15-21(2002).
RN [13]
RP IDENTIFICATION BY MASS SPECTROMETRY.
RC TISSUE=Lymphoblast;
RX PubMed=14654843; DOI=10.1038/nature02166;
RA Andersen J.S., Wilkinson C.J., Mayor T., Mortensen P., Nigg E.A., Mann M.;
RT "Proteomic characterization of the human centrosome by protein correlation
RT profiling.";
RL Nature 426:570-574(2003).
RN [14]
RP CHARACTERIZATION OF THE EIF-3 COMPLEX.
RX PubMed=15703437; DOI=10.1261/rna.7215305;
RA Kolupaeva V.G., Unbehaun A., Lomakin I.B., Hellen C.U.T., Pestova T.V.;
RT "Binding of eukaryotic initiation factor 3 to ribosomal 40S subunits and
RT its role in ribosomal dissociation and anti-association.";
RL RNA 11:470-486(2005).
RN [15]
RP INTERACTION WITH IFIT1.
RX PubMed=16023166; DOI=10.1016/j.virol.2005.06.011;
RA Terenzi F., Pal S., Sen G.C.;
RT "Induction and mode of action of the viral stress-inducible murine
RT proteins, P56 and P54.";
RL Virology 340:116-124(2005).
RN [16]
RP INTERACTION WITH EIF4G1, IDENTIFICATION IN THE EIF-3 COMPLEX, AND
RP IDENTIFICATION BY MASS SPECTROMETRY.
RX PubMed=16766523; DOI=10.1074/jbc.m605418200;
RA LeFebvre A.K., Korneeva N.L., Trutschl M., Cvek U., Duzan R.D.,
RA Bradley C.A., Hershey J.W.B., Rhoads R.E.;
RT "Translation initiation factor eIF4G-1 binds to eIF3 through the eIF3e
RT subunit.";
RL J. Biol. Chem. 281:22917-22932(2006).
RN [17]
RP INTERACTION WITH IFIT2.
RX PubMed=16973618; DOI=10.1074/jbc.m605771200;
RA Terenzi F., Hui D.J., Merrick W.C., Sen G.C.;
RT "Distinct induction patterns and functions of two closely related
RT interferon-inducible human genes, ISG54 and ISG56.";
RL J. Biol. Chem. 281:34064-34071(2006).
RN [18]
RP FUNCTION, AND CHARACTERIZATION OF THE EIF-3 COMPLEX.
RX PubMed=17581632; DOI=10.1038/sj.emboj.7601765;
RA Masutani M., Sonenberg N., Yokoyama S., Imataka H.;
RT "Reconstitution reveals the functional core of mammalian eIF3.";
RL EMBO J. 26:3373-3383(2007).
RN [19]
RP FUNCTION, AND INTERACTION WITH EIF3A; EIF3B; EIF3C; EIF4G1; NCBP1 AND UPF2.
RX PubMed=17468741; DOI=10.1038/sj.embor.7400955;
RA Morris C., Wittmann J., Jaeck H.-M., Jalinot P.;
RT "Human INT6/eIF3e is required for nonsense-mediated mRNA decay.";
RL EMBO Rep. 8:596-602(2007).
RN [20]
RP FUNCTION, AND INTERACTION WITH EPAS1.
RX PubMed=17324924; DOI=10.1074/jbc.m700423200;
RA Chen L., Uchida K., Endler A., Shibasaki F.;
RT "Mammalian tumor suppressor Int6 specifically targets hypoxia inducible
RT factor 2 alpha for degradation by hypoxia- and pVHL-independent
RT regulation.";
RL J. Biol. Chem. 282:12707-12716(2007).
RN [21]
RP SUBCELLULAR LOCATION, AND MUTAGENESIS OF LEU-312.
RX PubMed=17761670; DOI=10.1074/jbc.m706276200;
RA Sha Z., Yen H.-C.S., Scheel H., Suo J., Hofmann K., Chang E.C.;
RT "Isolation of the Schizosaccharomyces pombe proteasome subunit Rpn7 and a
RT structure-function study of the proteasome-COP9-initiation factor domain.";
RL J. Biol. Chem. 282:32414-32423(2007).
RN [22]
RP IDENTIFICATION IN THE EIF-3 COMPLEX, CHARACTERIZATION OF THE EIF-3 COMPLEX,
RP CLEAVAGE OF INITIATOR METHIONINE, ACETYLATION AT ALA-2, AND MASS
RP SPECTROMETRY.
RX PubMed=17322308; DOI=10.1074/mcp.m600399-mcp200;
RA Damoc E., Fraser C.S., Zhou M., Videler H., Mayeur G.L., Hershey J.W.B.,
RA Doudna J.A., Robinson C.V., Leary J.A.;
RT "Structural characterization of the human eukaryotic initiation factor 3
RT protein complex by mass spectrometry.";
RL Mol. Cell. Proteomics 6:1135-1146(2007).
RN [23]
RP FUNCTION, AND INTERACTION WITH MCM7.
RX PubMed=17310990; DOI=10.1038/sj.onc.1210314;
RA Buchsbaum S., Morris C., Bochard V., Jalinot P.;
RT "Human INT6 interacts with MCM7 and regulates its stability during S phase
RT of the cell cycle.";
RL Oncogene 26:5132-5144(2007).
RN [24]
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 [25]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-399, 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 [26]
RP IDENTIFICATION IN THE EIF-3 COMPLEX, CHARACTERIZATION OF THE EIF-3 COMPLEX,
RP MASS SPECTROMETRY, AND INTERACTION WITH EIF3B.
RX PubMed=18599441; DOI=10.1073/pnas.0801313105;
RA Zhou M., Sandercock A.M., Fraser C.S., Ridlova G., Stephens E.,
RA Schenauer M.R., Yokoi-Fong T., Barsky D., Leary J.A., Hershey J.W.B.,
RA Doudna J.A., Robinson C.V.;
RT "Mass spectrometry reveals modularity and a complete subunit interaction
RT map of the eukaryotic translation factor eIF3.";
RL Proc. Natl. Acad. Sci. U.S.A. 105:18139-18144(2008).
RN [27]
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 [28]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-399, AND IDENTIFICATION BY
RP MASS SPECTROMETRY [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 INTERACTION WITH BZW2/5MP1.
RX PubMed=21745818; DOI=10.1093/nar/gkr339;
RA Singh C.R., Watanabe R., Zhou D., Jennings M.D., Fukao A., Lee B.,
RA Ikeda Y., Chiorini J.A., Campbell S.G., Ashe M.P., Fujiwara T., Wek R.C.,
RA Pavitt G.D., Asano K.;
RT "Mechanisms of translational regulation by a human eIF5-mimic protein.";
RL Nucleic Acids Res. 39:8314-8328(2011).
RN [31]
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 [32]
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 [33]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-399, AND IDENTIFICATION BY
RP 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 [34]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-442, AND IDENTIFICATION BY
RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Liver;
RX PubMed=24275569; DOI=10.1016/j.jprot.2013.11.014;
RA Bian Y., Song C., Cheng K., Dong M., Wang F., Huang J., Sun D., Wang L.,
RA Ye M., Zou H.;
RT "An enzyme assisted RP-RPLC approach for in-depth analysis of human liver
RT phosphoproteome.";
RL J. Proteomics 96:253-262(2014).
RN [35]
RP FUNCTION, AND IDENTIFICATION IN THE EIF-3 COMPLEX.
RX PubMed=25849773; DOI=10.1038/nature14267;
RA Lee A.S., Kranzusch P.J., Cate J.H.;
RT "eIF3 targets cell-proliferation messenger RNAs for translational
RT activation or repression.";
RL Nature 522:111-114(2015).
RN [36]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=25944712; DOI=10.1002/pmic.201400617;
RA Vaca Jacome A.S., Rabilloud T., Schaeffer-Reiss C., Rompais M., Ayoub D.,
RA Lane L., Bairoch A., Van Dorsselaer A., Carapito C.;
RT "N-terminome analysis of the human mitochondrial proteome.";
RL Proteomics 15:2519-2524(2015).
RN [37]
RP FUNCTION.
RX PubMed=27462815; DOI=10.1038/nature18954;
RA Lee A.S., Kranzusch P.J., Doudna J.A., Cate J.H.;
RT "eIF3d is an mRNA cap-binding protein that is required for specialized
RT translation initiation.";
RL Nature 536:96-99(2016).
RN [38]
RP 3D-STRUCTURE MODELING, AND ELECTRON MICROSCOPY.
RX PubMed=16322461; DOI=10.1126/science.1118977;
RA Siridechadilok B., Fraser C.S., Hall R.J., Doudna J.A., Nogales E.;
RT "Structural roles for human translation factor eIF3 in initiation of
RT protein synthesis.";
RL Science 310:1513-1515(2005).
CC -!- FUNCTION: Component of the eukaryotic translation initiation factor 3
CC (eIF-3) complex, which is required for several steps in the initiation
CC of protein synthesis (PubMed:17581632, PubMed:25849773,
CC PubMed:27462815). The eIF-3 complex associates with the 40S ribosome
CC and facilitates the recruitment of eIF-1, eIF-1A, eIF-2:GTP:methionyl-
CC tRNAi and eIF-5 to form the 43S pre-initiation complex (43S PIC). The
CC eIF-3 complex stimulates mRNA recruitment to the 43S PIC and scanning
CC of the mRNA for AUG recognition. The eIF-3 complex is also required for
CC disassembly and recycling of post-termination ribosomal complexes and
CC subsequently prevents premature joining of the 40S and 60S ribosomal
CC subunits prior to initiation (PubMed:17581632). The eIF-3 complex
CC specifically targets and initiates translation of a subset of mRNAs
CC involved in cell proliferation, including cell cycling, differentiation
CC and apoptosis, and uses different modes of RNA stem-loop binding to
CC exert either translational activation or repression (PubMed:25849773).
CC Required for nonsense-mediated mRNA decay (NMD); may act in conjunction
CC with UPF2 to divert mRNAs from translation to the NMD pathway
CC (PubMed:17468741). May interact with MCM7 and EPAS1 and regulate the
CC proteasome-mediated degradation of these proteins (PubMed:17310990,
CC PubMed:17324924). {ECO:0000255|HAMAP-Rule:MF_03004,
CC ECO:0000269|PubMed:17310990, ECO:0000269|PubMed:17324924,
CC ECO:0000269|PubMed:17468741, ECO:0000269|PubMed:17581632,
CC ECO:0000269|PubMed:25849773, ECO:0000269|PubMed:27462815}.
CC -!- SUBUNIT: Component of the eukaryotic translation initiation factor 3
CC (eIF-3) complex, which is composed of 13 subunits: EIF3A, EIF3B, EIF3C,
CC EIF3D, EIF3E, EIF3F, EIF3G, EIF3H, EIF3I, EIF3J, EIF3K, EIF3L and
CC EIF3M. The eIF-3 complex appears to include 3 stable modules: module A
CC is composed of EIF3A, EIF3B, EIF3G and EIF3I; module B is composed of
CC EIF3F, EIF3H, and EIF3M; and module C is composed of EIF3C, EIF3D,
CC EIF3E, EIF3K and EIF3L. EIF3C of module C binds EIF3B of module A and
CC EIF3H of module B, thereby linking the three modules. EIF3J is a labile
CC subunit that binds to the eIF-3 complex via EIF3B. The eIF-3 complex
CC interacts with RPS6KB1 under conditions of nutrient depletion.
CC Mitogenic stimulation leads to binding and activation of a complex
CC composed of MTOR and RPTOR, leading to phosphorylation and release of
CC RPS6KB1 and binding of EIF4B to eIF-3. Interacts with COPS3, COPS6,
CC COPS7 (COPS7A or COPS7B), EIF4G1, EPAS1, MCM7, NCBP1, PSMC6, TRIM27 and
CC UPF2. Interacts with the HTLV-1 protein Tax-1. Interacts with IFIT1 and
CC IFIT2 (PubMed:16023166, PubMed:16973618). Interacts with BZW2/5MP1
CC (PubMed:21745818). {ECO:0000255|HAMAP-Rule:MF_03004,
CC ECO:0000269|PubMed:10504338, ECO:0000269|PubMed:11457827,
CC ECO:0000269|PubMed:11590142, ECO:0000269|PubMed:12220626,
CC ECO:0000269|PubMed:12386384, ECO:0000269|PubMed:16023166,
CC ECO:0000269|PubMed:16766523, ECO:0000269|PubMed:16973618,
CC ECO:0000269|PubMed:17310990, ECO:0000269|PubMed:17322308,
CC ECO:0000269|PubMed:17324924, ECO:0000269|PubMed:17468741,
CC ECO:0000269|PubMed:18599441, ECO:0000269|PubMed:21745818,
CC ECO:0000269|PubMed:25849773, ECO:0000269|PubMed:8688078,
CC ECO:0000269|PubMed:9295280}.
CC -!- INTERACTION:
CC P60228; Q8IY42: C4orf19; NbExp=4; IntAct=EBI-347740, EBI-10216552;
CC P60228; P04233: CD74; NbExp=2; IntAct=EBI-347740, EBI-2622890;
CC P60228; P02489: CRYAA; NbExp=3; IntAct=EBI-347740, EBI-6875961;
CC P60228; Q8IY21: DDX60; NbExp=2; IntAct=EBI-347740, EBI-2807346;
CC P60228; P55884: EIF3B; NbExp=6; IntAct=EBI-347740, EBI-366696;
CC P60228; Q99613: EIF3C; NbExp=14; IntAct=EBI-347740, EBI-353741;
CC P60228; O15371: EIF3D; NbExp=6; IntAct=EBI-347740, EBI-353818;
CC P60228; Q9UBQ5: EIF3K; NbExp=6; IntAct=EBI-347740, EBI-354344;
CC P60228; Q9Y262: EIF3L; NbExp=7; IntAct=EBI-347740, EBI-373519;
CC P60228; Q99814: EPAS1; NbExp=10; IntAct=EBI-347740, EBI-447470;
CC P60228; O95208-2: EPN2; NbExp=3; IntAct=EBI-347740, EBI-12135243;
CC P60228; Q5SUL5: HLA-A; NbExp=3; IntAct=EBI-347740, EBI-8561769;
CC P60228; Q86U28: ISCA2; NbExp=3; IntAct=EBI-347740, EBI-10258659;
CC P60228; Q92993: KAT5; NbExp=3; IntAct=EBI-347740, EBI-399080;
CC P60228; Q5T749: KPRP; NbExp=3; IntAct=EBI-347740, EBI-10981970;
CC P60228; Q8TAP4-4: LMO3; NbExp=3; IntAct=EBI-347740, EBI-11742507;
CC P60228; Q5JXC2: MIIP; NbExp=3; IntAct=EBI-347740, EBI-2801965;
CC P60228; Q6NTE8: MRNIP; NbExp=3; IntAct=EBI-347740, EBI-2857471;
CC P60228; P17252: PRKCA; NbExp=3; IntAct=EBI-347740, EBI-1383528;
CC P60228; Q59EK9: RUNDC3A; NbExp=4; IntAct=EBI-347740, EBI-747225;
CC P60228; Q59EK9-3: RUNDC3A; NbExp=3; IntAct=EBI-347740, EBI-11957366;
CC P60228; Q15047-2: SETDB1; NbExp=3; IntAct=EBI-347740, EBI-9090795;
CC P60228; P14373: TRIM27; NbExp=7; IntAct=EBI-347740, EBI-719493;
CC P60228; P61981: YWHAG; NbExp=3; IntAct=EBI-347740, EBI-359832;
CC P60228; Q8IUH5: ZDHHC17; NbExp=2; IntAct=EBI-347740, EBI-524753;
CC P60228; Q96MX3: ZNF48; NbExp=3; IntAct=EBI-347740, EBI-12006434;
CC P60228; Q9Q2G4: ORF; Xeno; NbExp=5; IntAct=EBI-347740, EBI-6248094;
CC -!- SUBCELLULAR LOCATION: Cytoplasm. Nucleus, PML body.
CC -!- TISSUE SPECIFICITY: Ubiquitously expressed. Expressed at highest levels
CC in appendix, lymph, pancreas, skeletal muscle, spleen and thymus.
CC {ECO:0000269|PubMed:8688078, ECO:0000269|PubMed:9295280}.
CC -!- MASS SPECTROMETRY: Mass=52131.8; Method=Unknown;
CC Evidence={ECO:0000269|PubMed:17322308};
CC -!- MASS SPECTROMETRY: Mass=52133.4; Mass_error=0.2; Method=MALDI;
CC Evidence={ECO:0000269|PubMed:18599441};
CC -!- SIMILARITY: Belongs to the eIF-3 subunit E family. {ECO:0000255|HAMAP-
CC Rule:MF_03004}.
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DR EMBL; U54562; AAC51760.1; -; mRNA.
DR EMBL; U94174; AAC51917.1; -; Genomic_DNA.
DR EMBL; U94162; AAC51917.1; JOINED; Genomic_DNA.
DR EMBL; U94163; AAC51917.1; JOINED; Genomic_DNA.
DR EMBL; U94164; AAC51917.1; JOINED; Genomic_DNA.
DR EMBL; U94165; AAC51917.1; JOINED; Genomic_DNA.
DR EMBL; U94166; AAC51917.1; JOINED; Genomic_DNA.
DR EMBL; U94167; AAC51917.1; JOINED; Genomic_DNA.
DR EMBL; U94168; AAC51917.1; JOINED; Genomic_DNA.
DR EMBL; U94169; AAC51917.1; JOINED; Genomic_DNA.
DR EMBL; U94170; AAC51917.1; JOINED; Genomic_DNA.
DR EMBL; U94171; AAC51917.1; JOINED; Genomic_DNA.
DR EMBL; U94172; AAC51917.1; JOINED; Genomic_DNA.
DR EMBL; U94173; AAC51917.1; JOINED; Genomic_DNA.
DR EMBL; U94175; AAC51919.1; -; mRNA.
DR EMBL; U62962; AAB58251.1; -; mRNA.
DR EMBL; U85947; AAB88873.1; -; mRNA.
DR EMBL; CR542275; CAG47071.1; -; mRNA.
DR EMBL; CH471060; EAW91918.1; -; Genomic_DNA.
DR EMBL; BC000734; AAH00734.1; -; mRNA.
DR EMBL; BC008419; AAH08419.1; -; mRNA.
DR EMBL; BC016706; AAH16706.1; -; mRNA.
DR EMBL; BC017887; AAH17887.1; -; mRNA.
DR EMBL; BC021679; AAH21679.1; -; mRNA.
DR CCDS; CCDS6308.1; -.
DR RefSeq; NP_001559.1; NM_001568.2.
DR PDB; 3J8B; EM; -; E=1-395.
DR PDB; 3J8C; EM; -; E=1-395.
DR PDB; 6FEC; EM; 6.30 A; 3=1-445.
DR PDB; 6YBD; EM; 3.30 A; v=1-445.
DR PDB; 6ZMW; EM; 3.70 A; v=1-445.
DR PDB; 6ZON; EM; 3.00 A; E=1-445.
DR PDB; 6ZP4; EM; 2.90 A; E=1-445.
DR PDB; 6ZVJ; EM; 3.80 A; E=2-430.
DR PDB; 7A09; EM; 3.50 A; E=1-445.
DR PDBsum; 3J8B; -.
DR PDBsum; 3J8C; -.
DR PDBsum; 6FEC; -.
DR PDBsum; 6YBD; -.
DR PDBsum; 6ZMW; -.
DR PDBsum; 6ZON; -.
DR PDBsum; 6ZP4; -.
DR PDBsum; 6ZVJ; -.
DR PDBsum; 7A09; -.
DR AlphaFoldDB; P60228; -.
DR SMR; P60228; -.
DR BioGRID; 109857; 200.
DR ComplexPortal; CPX-6036; Eukaryotic translation initiation factor 3 complex.
DR CORUM; P60228; -.
DR DIP; DIP-32691N; -.
DR IntAct; P60228; 100.
DR MINT; P60228; -.
DR STRING; 9606.ENSP00000220849; -.
DR GlyGen; P60228; 1 site, 1 O-linked glycan (1 site).
DR iPTMnet; P60228; -.
DR MetOSite; P60228; -.
DR PhosphoSitePlus; P60228; -.
DR SwissPalm; P60228; -.
DR BioMuta; EIF3E; -.
DR DMDM; 41019126; -.
DR EPD; P60228; -.
DR jPOST; P60228; -.
DR MassIVE; P60228; -.
DR MaxQB; P60228; -.
DR PaxDb; P60228; -.
DR PeptideAtlas; P60228; -.
DR PRIDE; P60228; -.
DR ProteomicsDB; 57190; -.
DR Antibodypedia; 13407; 304 antibodies from 33 providers.
DR DNASU; 3646; -.
DR Ensembl; ENST00000220849.10; ENSP00000220849.5; ENSG00000104408.11.
DR GeneID; 3646; -.
DR KEGG; hsa:3646; -.
DR MANE-Select; ENST00000220849.10; ENSP00000220849.5; NM_001568.3; NP_001559.1.
DR UCSC; uc003ymu.4; human.
DR CTD; 3646; -.
DR DisGeNET; 3646; -.
DR GeneCards; EIF3E; -.
DR HGNC; HGNC:3277; EIF3E.
DR HPA; ENSG00000104408; Low tissue specificity.
DR MIM; 602210; gene.
DR neXtProt; NX_P60228; -.
DR OpenTargets; ENSG00000104408; -.
DR PharmGKB; PA27705; -.
DR VEuPathDB; HostDB:ENSG00000104408; -.
DR eggNOG; KOG2758; Eukaryota.
DR GeneTree; ENSGT00390000002661; -.
DR InParanoid; P60228; -.
DR OMA; TWGKLAC; -.
DR OrthoDB; 1151808at2759; -.
DR PhylomeDB; P60228; -.
DR TreeFam; TF101518; -.
DR PathwayCommons; P60228; -.
DR Reactome; R-HSA-156827; L13a-mediated translational silencing of Ceruloplasmin expression.
DR Reactome; R-HSA-72649; Translation initiation complex formation.
DR Reactome; R-HSA-72689; Formation of a pool of free 40S subunits.
DR Reactome; R-HSA-72695; Formation of the ternary complex, and subsequently, the 43S complex.
DR Reactome; R-HSA-72702; Ribosomal scanning and start codon recognition.
DR Reactome; R-HSA-72706; GTP hydrolysis and joining of the 60S ribosomal subunit.
DR SignaLink; P60228; -.
DR SIGNOR; P60228; -.
DR BioGRID-ORCS; 3646; 658 hits in 1089 CRISPR screens.
DR ChiTaRS; EIF3E; human.
DR GeneWiki; EIF3S6; -.
DR GenomeRNAi; 3646; -.
DR Pharos; P60228; Tbio.
DR PRO; PR:P60228; -.
DR Proteomes; UP000005640; Chromosome 8.
DR RNAct; P60228; protein.
DR Bgee; ENSG00000104408; Expressed in calcaneal tendon and 209 other tissues.
DR ExpressionAtlas; P60228; baseline and differential.
DR Genevisible; P60228; HS.
DR GO; GO:0005737; C:cytoplasm; IDA:UniProtKB.
DR GO; GO:0005829; C:cytosol; IDA:HPA.
DR GO; GO:0016282; C:eukaryotic 43S preinitiation complex; IEA:UniProtKB-UniRule.
DR GO; GO:0033290; C:eukaryotic 48S preinitiation complex; IEA:UniProtKB-UniRule.
DR GO; GO:0005852; C:eukaryotic translation initiation factor 3 complex; IDA:UniProtKB.
DR GO; GO:0071540; C:eukaryotic translation initiation factor 3 complex, eIF3e; IEA:UniProtKB-UniRule.
DR GO; GO:0070062; C:extracellular exosome; HDA:UniProtKB.
DR GO; GO:0016020; C:membrane; HDA:UniProtKB.
DR GO; GO:0005654; C:nucleoplasm; NAS:UniProtKB.
DR GO; GO:0005634; C:nucleus; IDA:UniProtKB.
DR GO; GO:0016605; C:PML body; IEA:UniProtKB-SubCell.
DR GO; GO:0045296; F:cadherin binding; HDA:BHF-UCL.
DR GO; GO:0047485; F:protein N-terminus binding; IPI:UniProtKB.
DR GO; GO:0003723; F:RNA binding; HDA:UniProtKB.
DR GO; GO:0003743; F:translation initiation factor activity; IC:UniProtKB.
DR GO; GO:0001732; P:formation of cytoplasmic translation initiation complex; IC:ComplexPortal.
DR GO; GO:0045947; P:negative regulation of translational initiation; NAS:UniProtKB.
DR GO; GO:0000184; P:nuclear-transcribed mRNA catabolic process, nonsense-mediated decay; IMP:UniProtKB.
DR GO; GO:1902416; P:positive regulation of mRNA binding; IPI:ParkinsonsUK-UCL.
DR GO; GO:0045727; P:positive regulation of translation; IPI:ParkinsonsUK-UCL.
DR GO; GO:0006446; P:regulation of translational initiation; ISS:UniProtKB.
DR GO; GO:0006413; P:translational initiation; IDA:UniProtKB.
DR HAMAP; MF_03004; eIF3e; 1.
DR InterPro; IPR016650; eIF3e.
DR InterPro; IPR019010; eIF3e_N.
DR InterPro; IPR000717; PCI_dom.
DR InterPro; IPR036390; WH_DNA-bd_sf.
DR PANTHER; PTHR10317; PTHR10317; 1.
DR Pfam; PF09440; eIF3_N; 1.
DR Pfam; PF01399; PCI; 1.
DR PIRSF; PIRSF016255; eIF3e_su6; 1.
DR SMART; SM01186; eIF3_N; 1.
DR SMART; SM00088; PINT; 1.
DR SUPFAM; SSF46785; SSF46785; 1.
DR PROSITE; PS50250; PCI; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Acetylation; Cytoplasm; Direct protein sequencing;
KW Initiation factor; Nucleus; Phosphoprotein; Protein biosynthesis;
KW Reference proteome.
FT INIT_MET 1
FT /note="Removed"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_03004,
FT ECO:0000269|PubMed:17322308, ECO:0000269|Ref.8,
FT ECO:0007744|PubMed:19413330, ECO:0007744|PubMed:22223895,
FT ECO:0007744|PubMed:22814378"
FT CHAIN 2..445
FT /note="Eukaryotic translation initiation factor 3 subunit
FT E"
FT /id="PRO_0000123515"
FT DOMAIN 221..398
FT /note="PCI"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01185"
FT REGION 4..128
FT /note="Sufficient for interaction with EPAS1"
FT /evidence="ECO:0000269|PubMed:17324924"
FT REGION 9..195
FT /note="Sufficient for interaction with TRIM27"
FT /evidence="ECO:0000269|PubMed:10504338"
FT REGION 351..445
FT /note="Sufficient for interaction with MCM7"
FT /evidence="ECO:0000269|PubMed:17310990"
FT MOD_RES 2
FT /note="N-acetylalanine"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_03004,
FT ECO:0000269|PubMed:17322308, ECO:0000269|Ref.8,
FT ECO:0007744|PubMed:19413330, ECO:0007744|PubMed:22223895,
FT ECO:0007744|PubMed:22814378"
FT MOD_RES 399
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:18669648,
FT ECO:0007744|PubMed:20068231, ECO:0007744|PubMed:23186163"
FT MOD_RES 439
FT /note="Phosphothreonine"
FT /evidence="ECO:0000250|UniProtKB:P60229"
FT MOD_RES 442
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:24275569"
FT MOD_RES 445
FT /note="Phosphotyrosine"
FT /evidence="ECO:0000250|UniProtKB:P60229"
FT VARIANT 185
FT /note="A -> V (in dbSNP:rs17856554)"
FT /evidence="ECO:0000269|PubMed:15489334"
FT /id="VAR_046480"
FT MUTAGEN 312
FT /note="L->D: Promotes nuclear accumulation."
FT /evidence="ECO:0000269|PubMed:17761670"
FT STRAND 35..37
FT /evidence="ECO:0007829|PDB:6YBD"
FT HELIX 38..41
FT /evidence="ECO:0007829|PDB:6YBD"
FT HELIX 50..54
FT /evidence="ECO:0007829|PDB:6YBD"
FT HELIX 62..65
FT /evidence="ECO:0007829|PDB:6YBD"
FT HELIX 67..69
FT /evidence="ECO:0007829|PDB:6YBD"
FT STRAND 73..75
FT /evidence="ECO:0007829|PDB:6YBD"
FT HELIX 77..82
FT /evidence="ECO:0007829|PDB:6YBD"
FT TURN 85..88
FT /evidence="ECO:0007829|PDB:6YBD"
FT TURN 94..96
FT /evidence="ECO:0007829|PDB:6YBD"
FT HELIX 97..105
FT /evidence="ECO:0007829|PDB:6YBD"
FT HELIX 106..108
FT /evidence="ECO:0007829|PDB:6YBD"
FT TURN 109..112
FT /evidence="ECO:0007829|PDB:6YBD"
FT TURN 126..128
FT /evidence="ECO:0007829|PDB:6YBD"
FT HELIX 129..137
FT /evidence="ECO:0007829|PDB:6YBD"
FT TURN 148..152
FT /evidence="ECO:0007829|PDB:6YBD"
FT HELIX 165..176
FT /evidence="ECO:0007829|PDB:6YBD"
FT TURN 177..180
FT /evidence="ECO:0007829|PDB:6YBD"
FT HELIX 182..194
FT /evidence="ECO:0007829|PDB:6YBD"
FT HELIX 204..217
FT /evidence="ECO:0007829|PDB:6YBD"
FT STRAND 222..224
FT /evidence="ECO:0007829|PDB:6YBD"
FT HELIX 225..228
FT /evidence="ECO:0007829|PDB:6YBD"
FT HELIX 229..231
FT /evidence="ECO:0007829|PDB:6YBD"
FT TURN 232..234
FT /evidence="ECO:0007829|PDB:6YBD"
FT HELIX 238..244
FT /evidence="ECO:0007829|PDB:6YBD"
FT TURN 245..248
FT /evidence="ECO:0007829|PDB:6YBD"
FT HELIX 251..263
FT /evidence="ECO:0007829|PDB:6YBD"
FT TURN 271..275
FT /evidence="ECO:0007829|PDB:6YBD"
FT HELIX 276..279
FT /evidence="ECO:0007829|PDB:6YBD"
FT TURN 280..284
FT /evidence="ECO:0007829|PDB:6YBD"
FT TURN 291..296
FT /evidence="ECO:0007829|PDB:6YBD"
FT TURN 299..301
FT /evidence="ECO:0007829|PDB:6YBD"
FT HELIX 305..307
FT /evidence="ECO:0007829|PDB:6YBD"
FT STRAND 308..312
FT /evidence="ECO:0007829|PDB:6YBD"
FT HELIX 315..320
FT /evidence="ECO:0007829|PDB:6YBD"
FT STRAND 325..328
FT /evidence="ECO:0007829|PDB:6YBD"
FT HELIX 330..347
FT /evidence="ECO:0007829|PDB:6YBD"
FT STRAND 348..350
FT /evidence="ECO:0007829|PDB:6YBD"
FT HELIX 353..356
FT /evidence="ECO:0007829|PDB:6YBD"
FT TURN 359..361
FT /evidence="ECO:0007829|PDB:6YBD"
FT HELIX 364..376
FT /evidence="ECO:0007829|PDB:6YBD"
FT TURN 377..379
FT /evidence="ECO:0007829|PDB:6YBD"
FT TURN 399..402
FT /evidence="ECO:0007829|PDB:6YBD"
FT HELIX 403..419
FT /evidence="ECO:0007829|PDB:6YBD"
SQ SEQUENCE 445 AA; 52221 MW; A5368651DD0DDD0C CRC64;
MAEYDLTTRI AHFLDRHLVF PLLEFLSVKE IYNEKELLQG KLDLLSDTNM VDFAMDVYKN
LYSDDIPHAL REKRTTVVAQ LKQLQAETEP IVKMFEDPET TRQMQSTRDG RMLFDYLADK
HGFRQEYLDT LYRYAKFQYE CGNYSGAAEY LYFFRVLVPA TDRNALSSLW GKLASEILMQ
NWDAAMEDLT RLKETIDNNS VSSPLQSLQQ RTWLIHWSLF VFFNHPKGRD NIIDLFLYQP
QYLNAIQTMC PHILRYLTTA VITNKDVRKR RQVLKDLVKV IQQESYTYKD PITEFVECLY
VNFDFDGAQK KLRECESVLV NDFFLVACLE DFIENARLFI FETFCRIHQC ISINMLADKL
NMTPEEAERW IVNLIRNARL DAKIDSKLGH VVMGNNAVSP YQQVIEKTKS LSFRSQMLAM
NIEKKLNQNS RSEAPNWATQ DSGFY
