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 02-SEP-2026, entry version 210. 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}, INT6 GN {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; 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; Q14152: EIF3A; NbExp=18; IntAct=EBI-347740, EBI-366617; CC P60228; P55884: EIF3B; NbExp=9; IntAct=EBI-347740, EBI-366696; CC P60228; Q99613: EIF3C; NbExp=16; IntAct=EBI-347740, EBI-353741; CC P60228; O15371: EIF3D; NbExp=8; IntAct=EBI-347740, EBI-353818; CC P60228; Q9UBQ5: EIF3K; NbExp=9; IntAct=EBI-347740, EBI-354344; CC P60228; Q9Y262: EIF3L; NbExp=9; 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; Q9HC44: GPBP1L1; NbExp=4; IntAct=EBI-347740, EBI-746674; 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; P06748: NPM1; NbExp=3; IntAct=EBI-347740, EBI-78579; CC P60228; Q8IY42: PGCKA1; NbExp=4; IntAct=EBI-347740, EBI-10216552; 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}. CC --------------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution (CC BY 4.0) License CC --------------------------------------------------------------------------- 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_001568.3. 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 PDB; 7QP6; EM; 4.70 A; v=1-445. DR PDB; 7QP7; EM; 3.70 A; v=1-445. DR PDB; 8OZ0; EM; 3.50 A; 5=1-445. DR PDB; 8PJ1; EM; 3.40 A; v=1-445. DR PDB; 8PJ2; EM; 3.40 A; v=1-445. DR PDB; 8PJ3; EM; 3.70 A; v=1-445. DR PDB; 8PJ4; EM; 3.20 A; v=1-445. DR PDB; 8PJ5; EM; 2.90 A; v=1-445. DR PDB; 8PJ6; EM; 2.90 A; v=1-445. DR PDB; 8PPL; EM; 2.65 A; Iv=1-445. DR PDB; 8RG0; EM; 3.40 A; v=1-445. DR PDB; 8XXN; EM; 3.60 A; 3E=1-445. DR PDB; 9BLN; EM; 3.90 A; v=1-445. DR PDB; 9KKF; EM; 3.30 A; 3e=1-445. DR PDB; 9KN5; EM; 3.20 A; 3e=1-445. DR PDB; 9KN6; EM; 3.30 A; 3e=1-445. DR PDB; 9KRP; EM; 3.20 A; 3e=1-445. DR PDB; 9KZU; EM; 3.00 A; 3e=1-445. DR PDB; 9KZX; EM; 3.30 A; 3e=1-445. DR AlphaFoldDB; P60228; -. DR EMDB; EMD-10769; -. DR EMDB; EMD-11302; -. DR EMDB; EMD-11325; -. DR EMDB; EMD-11335; -. DR EMDB; EMD-11458; -. DR EMDB; EMD-11602; -. DR EMDB; EMD-14113; -. DR EMDB; EMD-14114; -. DR EMDB; EMD-17297; -. DR EMDB; EMD-17696; -. DR EMDB; EMD-17697; -. DR EMDB; EMD-17698; -. DR EMDB; EMD-17699; -. DR EMDB; EMD-17700; -. DR EMDB; EMD-17701; -. DR EMDB; EMD-17805; -. DR EMDB; EMD-19128; -. DR EMDB; EMD-38754; -. DR EMDB; EMD-4242; -. DR EMDB; EMD-44671; -. DR EMDB; EMD-62386; -. DR EMDB; EMD-62453; -. DR EMDB; EMD-62454; -. DR EMDB; EMD-62535; -. DR EMDB; EMD-62671; -. DR EMDB; EMD-62679; -. DR SMR; P60228; -. DR BioGRID; 109857; 305. DR ComplexPortal; CPX-6036; Eukaryotic translation initiation factor 3 complex. DR CORUM; P60228; -. DR DIP; DIP-32691N; -. DR FunCoup; P60228; 3597. DR IntAct; P60228; 150. DR MINT; P60228; -. DR NDEx; IQUERY-CP-EIF3E; 5 NDEx IQuery Curated Pathways. DR STRING; 9606.ENSP00000220849; -. DR BindingDB; P60228; -. DR ChEMBL; CHEMBL5725122; -. 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 jPOST; P60228; -. DR MassIVE; P60228; -. DR PaxDb; 9606-ENSP00000220849; -. DR PeptideAtlas; P60228; -. DR ProteomicsDB; 57190; -. DR Pumba; P60228; -. DR Antibodypedia; 13407; 312 antibodies from 36 providers. DR DNASU; 3646; -. DR Ensembl; ENST00000220849.10; ENSP00000220849.5; ENSG00000104408.12. 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 AGR; HGNC:3277; -. DR ClinPGx; PA27705; -. DR CTD; 3646; -. DR DisGeNET; 3646; -. DR GeneCards; EIF3E; -. DR HGNC; HGNC:3277; EIF3E. DR HPA; ENSG00000104408; Low tissue specificity. DR MalaCards; EIF3E; -. DR MIM; 602210; gene. DR OpenTargets; ENSG00000104408; -. DR VEuPathDB; HostDB:ENSG00000104408; -. DR eggNOG; KOG2758; Eukaryota. DR GeneTree; ENSGT00390000002661; -. DR InParanoid; P60228; -. DR OMA; NCPWILR; -. DR OrthoDB; 417252at2759; -. DR PAN-GO; P60228; 3 GO annotations based on evolutionary models. DR PhylomeDB; P60228; -. 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 Agora; ENSG00000104408; -. DR BioGRID-ORCS; 3646; 690 hits in 1167 CRISPR screens. DR CD-CODE; 91857CE7; Nucleolus. DR CD-CODE; DEE660B4; Stress granule. DR ChiTaRS; EIF3E; human. DR EvolutionaryTrace; P60228; -. 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 211 other cell types or tissues. DR ExpressionAtlas; P60228; baseline and differential. DR GO; GO:0000785; C:chromatin; NAS:UniProtKB. 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; IBA:GO_Central. 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:0014069; C:postsynaptic density; IEA:Ensembl. DR GO; GO:0045296; F:cadherin binding; HDA:BHF-UCL. 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; NAS: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: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 CDD; cd21378; eIF3E; 1. 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; EUKARYOTIC TRANSLATION INITIATION FACTOR 3 SUBUNIT E; 1. DR Pfam; PF09440; eIF3_N; 1. DR Pfam; PF21357; EIF3E_C; 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; Winged helix' DNA-binding domain; 1. DR PROSITE; PS50250; PCI; 1. 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 PDBsum; 7QP6; -. DR PDBsum; 7QP7; -. DR PDBsum; 8OZ0; -. DR PDBsum; 8PJ1; -. DR PDBsum; 8PJ2; -. DR PDBsum; 8PJ3; -. DR PDBsum; 8PJ4; -. DR PDBsum; 8PJ5; -. DR PDBsum; 8PJ6; -. DR PDBsum; 8PPL; -. DR PDBsum; 8RG0; -. DR PDBsum; 8XXN; -. DR PDBsum; 9BLN; -. DR PDBsum; 9KKF; -. DR PDBsum; 9KN5; -. DR PDBsum; 9KN6; -. DR PDBsum; 9KRP; -. DR PDBsum; 9KZU; -. DR PDBsum; 9KZX; -. PE 1: Evidence at protein level; KW 3D-structure; Acetylation; Cytoplasm; Direct protein sequencing; KW Initiation factor; Nucleus; Phosphoprotein; Protein biosynthesis; KW Proteomics identification; 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 HELIX 2..4 FT /evidence="ECO:0007829|PDB:8PPL" FT HELIX 7..11 FT /evidence="ECO:0007829|PDB:8PPL" FT HELIX 16..29 FT /evidence="ECO:0007829|PDB:8PPL" FT HELIX 34..46 FT /evidence="ECO:0007829|PDB:8PPL" FT STRAND 47..49 FT /evidence="ECO:0007829|PDB:8PPL" FT HELIX 51..61 FT /evidence="ECO:0007829|PDB:8PPL" FT HELIX 65..67 FT /evidence="ECO:0007829|PDB:8PPL" FT HELIX 68..96 FT /evidence="ECO:0007829|PDB:8PPL" FT HELIX 98..106 FT /evidence="ECO:0007829|PDB:8PPL" FT HELIX 110..121 FT /evidence="ECO:0007829|PDB:8PPL" FT STRAND 122..124 FT /evidence="ECO:0007829|PDB:8PJ2" FT HELIX 125..140 FT /evidence="ECO:0007829|PDB:8PPL" FT HELIX 144..157 FT /evidence="ECO:0007829|PDB:8PPL" FT TURN 161..163 FT /evidence="ECO:0007829|PDB:6ZON" FT HELIX 164..178 FT /evidence="ECO:0007829|PDB:8PPL" FT HELIX 182..198 FT /evidence="ECO:0007829|PDB:8PPL" FT HELIX 204..224 FT /evidence="ECO:0007829|PDB:8PPL" FT HELIX 228..237 FT /evidence="ECO:0007829|PDB:8PPL" FT HELIX 240..248 FT /evidence="ECO:0007829|PDB:8PPL" FT HELIX 253..263 FT /evidence="ECO:0007829|PDB:8PPL" FT HELIX 267..283 FT /evidence="ECO:0007829|PDB:8PPL" FT TURN 284..287 FT /evidence="ECO:0007829|PDB:8PPL" FT HELIX 291..300 FT /evidence="ECO:0007829|PDB:8PPL" FT HELIX 305..321 FT /evidence="ECO:0007829|PDB:8PPL" FT TURN 323..325 FT /evidence="ECO:0007829|PDB:8PPL" FT HELIX 329..347 FT /evidence="ECO:0007829|PDB:8PPL" FT STRAND 349..352 FT /evidence="ECO:0007829|PDB:8PPL" FT HELIX 353..359 FT /evidence="ECO:0007829|PDB:8PPL" FT HELIX 364..377 FT /evidence="ECO:0007829|PDB:8PPL" FT STRAND 383..385 FT /evidence="ECO:0007829|PDB:8PPL" FT TURN 386..389 FT /evidence="ECO:0007829|PDB:8PPL" FT STRAND 390..392 FT /evidence="ECO:0007829|PDB:8PPL" FT HELIX 399..429 FT /evidence="ECO:0007829|PDB:8PPL" 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 //