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Eukaryotic translation initiation factor 3 subunit E (eIF3e) (Eukaryotic translation initiation factor 3 subunit 6) (Viral integration site protein INT-6 homolog) (eIF-3 p48)

 EIF3E_HUMAN             Reviewed;         445 AA.
P60228; O43902; Q64058; Q64059; Q64252; Q6FG33; Q8WVK4;
16-JAN-2004, integrated into UniProtKB/Swiss-Prot.
16-JAN-2004, sequence version 1.
12-SEP-2018, entry version 166.
RecName: Full=Eukaryotic translation initiation factor 3 subunit E {ECO:0000255|HAMAP-Rule:MF_03004};
Short=eIF3e {ECO:0000255|HAMAP-Rule:MF_03004};
AltName: Full=Eukaryotic translation initiation factor 3 subunit 6 {ECO:0000255|HAMAP-Rule:MF_03004};
AltName: Full=Viral integration site protein INT-6 homolog;
AltName: Full=eIF-3 p48 {ECO:0000255|HAMAP-Rule:MF_03004};
Name=EIF3E {ECO:0000255|HAMAP-Rule:MF_03004};
Synonyms=EIF3S6 {ECO:0000255|HAMAP-Rule:MF_03004},
INT6 {ECO:0000255|HAMAP-Rule:MF_03004};
Homo sapiens (Human).
Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
Catarrhini; Hominidae; Homo.
NCBI_TaxID=9606;
[1]
NUCLEOTIDE SEQUENCE [MRNA], PROTEIN SEQUENCE OF 280-289 AND 427-436,
INTERACTION WITH EIF3A, IDENTIFICATION IN THE EIF-3 COMPLEX, AND
TISSUE SPECIFICITY.
TISSUE=Liver;
PubMed=9295280; DOI=10.1074/jbc.272.38.23477;
Asano K., Merrick W.C., Hershey J.W.B.;
"The translation initiation factor eIF3-p48 subunit is encoded by int-
6, a site of frequent integration by the mouse mammary tumor virus
genome.";
J. Biol. Chem. 272:23477-23480(1997).
[2]
NUCLEOTIDE SEQUENCE [GENOMIC DNA / MRNA].
TISSUE=Lung;
PubMed=9403073; DOI=10.1006/geno.1997.4996;
Miyazaki S., Imatani A., Ballard L., Marchetti A., Buttitta F.,
Albertsen H., Nevanlinna H.A., Gallahan D., Callahan R.;
"The chromosome location of the human homolog of the mouse mammary
tumor-associated gene INT6 and its status in human breast
carcinomas.";
Genomics 46:155-158(1997).
[3]
NUCLEOTIDE SEQUENCE [MRNA], INTERACTION WITH TAX-1, SUBCELLULAR
LOCATION, AND TISSUE SPECIFICITY.
PubMed=8688078; DOI=10.1126/science.273.5277.951;
Desbois C., Rousset R., Bantignies F., Jalinot P.;
"Exclusion of Int-6 from PML nuclear bodies by binding to the HTLV-I
Tax oncoprotein.";
Science 273:951-953(1996).
[4]
NUCLEOTIDE SEQUENCE [MRNA], INTERACTION WITH TAX-1, AND SUBCELLULAR
LOCATION.
PubMed=12386384; DOI=10.1007/BF02253422;
Neuvert C., Jin D.-Y., Semmes O.J., Diella F., Callahan R.,
Jeang K.-T.;
"Divergent subcellular locations of HTLV-I Tax and Int-6: a contrast
between in vitro protein-protein binding and intracellular protein
colocalization.";
J. Biomed. Sci. 4:229-234(1997).
[5]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
Ebert L., Schick M., Neubert P., Schatten R., Henze S., Korn B.;
"Cloning of human full open reading frames in Gateway(TM) system entry
vector (pDONR201).";
Submitted (JUN-2004) to the EMBL/GenBank/DDBJ databases.
[6]
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Mural R.J., Istrail S., Sutton G.G., Florea L., Halpern A.L.,
Mobarry C.M., Lippert R., Walenz B., Shatkay H., Dew I., Miller J.R.,
Flanigan M.J., Edwards N.J., Bolanos R., Fasulo D., Halldorsson B.V.,
Hannenhalli S., Turner R., Yooseph S., Lu F., Nusskern D.R.,
Shue B.C., Zheng X.H., Zhong F., Delcher A.L., Huson D.H.,
Kravitz S.A., Mouchard L., Reinert K., Remington K.A., Clark A.G.,
Waterman M.S., Eichler E.E., Adams M.D., Hunkapiller M.W., Myers E.W.,
Venter J.C.;
Submitted (JUL-2005) to the EMBL/GenBank/DDBJ databases.
[7]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA], AND VARIANT VAL-185.
TISSUE=Bone marrow, Brain, Lung, and Muscle;
PubMed=15489334; DOI=10.1101/gr.2596504;
The MGC Project Team;
"The status, quality, and expansion of the NIH full-length cDNA
project: the Mammalian Gene Collection (MGC).";
Genome Res. 14:2121-2127(2004).
[8]
PROTEIN SEQUENCE OF 2-9; 60-71; 164-172; 256-265 AND 370-376, CLEAVAGE
OF INITIATOR METHIONINE, ACETYLATION AT ALA-2, AND IDENTIFICATION BY
MASS SPECTROMETRY.
TISSUE=Colon carcinoma, and Mammary carcinoma;
Bienvenut W.V., Heiserich L., Gottlieb E., Matallanas D., Cooper W.N.,
Kolch W.;
Submitted (MAR-2008) to UniProtKB.
[9]
INTERACTION WITH EIF3C AND TRIM27, AND SUBCELLULAR LOCATION.
PubMed=10504338;
Morris-Desbois C., Bochard V., Reynaud C., Jalinot P.;
"Interaction between the Ret finger protein and the Int-6 gene product
and co-localisation into nuclear bodies.";
J. Cell Sci. 112:3331-3342(1999).
[10]
INTERACTION WITH EIF3B.
PubMed=11457827; DOI=10.1074/jbc.M102161200;
Shalev A., Valasek L., Pise-Masison C.A., Radonovich M., Phan L.,
Clayton J., He H., Brady J.N., Hinnebusch A.G., Asano K.;
"Saccharomyces cerevisiae protein Pci8p and human protein eIF3e/Int-6
interact with the eIF3 core complex by binding to cognate eIF3b
subunits.";
J. Biol. Chem. 276:34948-34957(2001).
[11]
INTERACTION WITH EIF3L.
PubMed=11590142; DOI=10.1074/jbc.M104966200;
Morris-Desbois C., Rety S., Ferro M., Garin J., Jalinot P.;
"The human protein HSPC021 interacts with Int-6 and is associated with
eukaryotic translation initiation factor 3.";
J. Biol. Chem. 276:45988-45995(2001).
[12]
INTERACTION WITH COPS3; COPS6; COPS7 AND PSMC6.
PubMed=12220626; DOI=10.1016/S0014-5793(02)03147-2;
Hoareau Alves K., Bochard V., Rety S., Jalinot P.;
"Association of the mammalian proto-oncoprotein Int-6 with the three
protein complexes eIF3, COP9 signalosome and 26S proteasome.";
FEBS Lett. 527:15-21(2002).
[13]
CHARACTERIZATION OF THE EIF-3 COMPLEX.
PubMed=15703437; DOI=10.1261/rna.7215305;
Kolupaeva V.G., Unbehaun A., Lomakin I.B., Hellen C.U.T.,
Pestova T.V.;
"Binding of eukaryotic initiation factor 3 to ribosomal 40S subunits
and its role in ribosomal dissociation and anti-association.";
RNA 11:470-486(2005).
[14]
INTERACTION WITH IFIT1.
PubMed=16023166; DOI=10.1016/j.virol.2005.06.011;
Terenzi F., Pal S., Sen G.C.;
"Induction and mode of action of the viral stress-inducible murine
proteins, P56 and P54.";
Virology 340:116-124(2005).
[15]
INTERACTION WITH EIF4G1, IDENTIFICATION IN THE EIF-3 COMPLEX, AND
IDENTIFICATION BY MASS SPECTROMETRY.
PubMed=16766523; DOI=10.1074/jbc.M605418200;
LeFebvre A.K., Korneeva N.L., Trutschl M., Cvek U., Duzan R.D.,
Bradley C.A., Hershey J.W.B., Rhoads R.E.;
"Translation initiation factor eIF4G-1 binds to eIF3 through the eIF3e
subunit.";
J. Biol. Chem. 281:22917-22932(2006).
[16]
INTERACTION WITH IFIT2.
PubMed=16973618; DOI=10.1074/jbc.M605771200;
Terenzi F., Hui D.J., Merrick W.C., Sen G.C.;
"Distinct induction patterns and functions of two closely related
interferon-inducible human genes, ISG54 and ISG56.";
J. Biol. Chem. 281:34064-34071(2006).
[17]
FUNCTION, AND CHARACTERIZATION OF THE EIF-3 COMPLEX.
PubMed=17581632; DOI=10.1038/sj.emboj.7601765;
Masutani M., Sonenberg N., Yokoyama S., Imataka H.;
"Reconstitution reveals the functional core of mammalian eIF3.";
EMBO J. 26:3373-3383(2007).
[18]
FUNCTION, AND INTERACTION WITH EIF3A; EIF3B; EIF3C; EIF4G1; NCBP1 AND
UPF2.
PubMed=17468741; DOI=10.1038/sj.embor.7400955;
Morris C., Wittmann J., Jaeck H.-M., Jalinot P.;
"Human INT6/eIF3e is required for nonsense-mediated mRNA decay.";
EMBO Rep. 8:596-602(2007).
[19]
FUNCTION, AND INTERACTION WITH EPAS1.
PubMed=17324924; DOI=10.1074/jbc.M700423200;
Chen L., Uchida K., Endler A., Shibasaki F.;
"Mammalian tumor suppressor Int6 specifically targets hypoxia
inducible factor 2 alpha for degradation by hypoxia- and pVHL-
independent regulation.";
J. Biol. Chem. 282:12707-12716(2007).
[20]
SUBCELLULAR LOCATION, AND MUTAGENESIS OF LEU-312.
PubMed=17761670; DOI=10.1074/jbc.M706276200;
Sha Z., Yen H.-C.S., Scheel H., Suo J., Hofmann K., Chang E.C.;
"Isolation of the Schizosaccharomyces pombe proteasome subunit Rpn7
and a structure-function study of the proteasome-COP9-initiation
factor domain.";
J. Biol. Chem. 282:32414-32423(2007).
[21]
IDENTIFICATION IN THE EIF-3 COMPLEX, CHARACTERIZATION OF THE EIF-3
COMPLEX, CLEAVAGE OF INITIATOR METHIONINE, ACETYLATION AT ALA-2, AND
MASS SPECTROMETRY.
PubMed=17322308; DOI=10.1074/mcp.M600399-MCP200;
Damoc E., Fraser C.S., Zhou M., Videler H., Mayeur G.L.,
Hershey J.W.B., Doudna J.A., Robinson C.V., Leary J.A.;
"Structural characterization of the human eukaryotic initiation factor
3 protein complex by mass spectrometry.";
Mol. Cell. Proteomics 6:1135-1146(2007).
[22]
FUNCTION, AND INTERACTION WITH MCM7.
PubMed=17310990; DOI=10.1038/sj.onc.1210314;
Buchsbaum S., Morris C., Bochard V., Jalinot P.;
"Human INT6 interacts with MCM7 and regulates its stability during S
phase of the cell cycle.";
Oncogene 26:5132-5144(2007).
[23]
IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
TISSUE=Cervix carcinoma;
PubMed=18691976; DOI=10.1016/j.molcel.2008.07.007;
Daub H., Olsen J.V., Bairlein M., Gnad F., Oppermann F.S., Korner R.,
Greff Z., Keri G., Stemmann O., Mann M.;
"Kinase-selective enrichment enables quantitative phosphoproteomics of
the kinome across the cell cycle.";
Mol. Cell 31:438-448(2008).
[24]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-399, AND IDENTIFICATION
BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
TISSUE=Cervix carcinoma;
PubMed=18669648; DOI=10.1073/pnas.0805139105;
Dephoure N., Zhou C., Villen J., Beausoleil S.A., Bakalarski C.E.,
Elledge S.J., Gygi S.P.;
"A quantitative atlas of mitotic phosphorylation.";
Proc. Natl. Acad. Sci. U.S.A. 105:10762-10767(2008).
[25]
IDENTIFICATION IN THE EIF-3 COMPLEX, CHARACTERIZATION OF THE EIF-3
COMPLEX, MASS SPECTROMETRY, AND INTERACTION WITH EIF3B.
PubMed=18599441; DOI=10.1073/pnas.0801313105;
Zhou M., Sandercock A.M., Fraser C.S., Ridlova G., Stephens E.,
Schenauer M.R., Yokoi-Fong T., Barsky D., Leary J.A., Hershey J.W.B.,
Doudna J.A., Robinson C.V.;
"Mass spectrometry reveals modularity and a complete subunit
interaction map of the eukaryotic translation factor eIF3.";
Proc. Natl. Acad. Sci. U.S.A. 105:18139-18144(2008).
[26]
ACETYLATION [LARGE SCALE ANALYSIS] AT ALA-2, CLEAVAGE OF INITIATOR
METHIONINE [LARGE SCALE ANALYSIS], AND IDENTIFICATION BY MASS
SPECTROMETRY [LARGE SCALE ANALYSIS].
PubMed=19413330; DOI=10.1021/ac9004309;
Gauci S., Helbig A.O., Slijper M., Krijgsveld J., Heck A.J.,
Mohammed S.;
"Lys-N and trypsin cover complementary parts of the phosphoproteome in
a refined SCX-based approach.";
Anal. Chem. 81:4493-4501(2009).
[27]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-399, AND IDENTIFICATION
BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
TISSUE=Cervix carcinoma;
PubMed=20068231; DOI=10.1126/scisignal.2000475;
Olsen J.V., Vermeulen M., Santamaria A., Kumar C., Miller M.L.,
Jensen L.J., Gnad F., Cox J., Jensen T.S., Nigg E.A., Brunak S.,
Mann M.;
"Quantitative phosphoproteomics reveals widespread full
phosphorylation site occupancy during mitosis.";
Sci. Signal. 3:RA3-RA3(2010).
[28]
IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
PubMed=21269460; DOI=10.1186/1752-0509-5-17;
Burkard T.R., Planyavsky M., Kaupe I., Breitwieser F.P.,
Buerckstuemmer T., Bennett K.L., Superti-Furga G., Colinge J.;
"Initial characterization of the human central proteome.";
BMC Syst. Biol. 5:17-17(2011).
[29]
ACETYLATION [LARGE SCALE ANALYSIS] AT ALA-2, CLEAVAGE OF INITIATOR
METHIONINE [LARGE SCALE ANALYSIS], AND IDENTIFICATION BY MASS
SPECTROMETRY [LARGE SCALE ANALYSIS].
PubMed=22223895; DOI=10.1074/mcp.M111.015131;
Bienvenut W.V., Sumpton D., Martinez A., Lilla S., Espagne C.,
Meinnel T., Giglione C.;
"Comparative large-scale characterisation of plant vs. mammal proteins
reveals similar and idiosyncratic N-alpha acetylation features.";
Mol. Cell. Proteomics 11:M111.015131-M111.015131(2012).
[30]
ACETYLATION [LARGE SCALE ANALYSIS] AT ALA-2, CLEAVAGE OF INITIATOR
METHIONINE [LARGE SCALE ANALYSIS], AND IDENTIFICATION BY MASS
SPECTROMETRY [LARGE SCALE ANALYSIS].
PubMed=22814378; DOI=10.1073/pnas.1210303109;
Van Damme P., Lasa M., Polevoda B., Gazquez C., Elosegui-Artola A.,
Kim D.S., De Juan-Pardo E., Demeyer K., Hole K., Larrea E.,
Timmerman E., Prieto J., Arnesen T., Sherman F., Gevaert K.,
Aldabe R.;
"N-terminal acetylome analyses and functional insights of the N-
terminal acetyltransferase NatB.";
Proc. Natl. Acad. Sci. U.S.A. 109:12449-12454(2012).
[31]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-399, AND IDENTIFICATION
BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
TISSUE=Cervix carcinoma, and Erythroleukemia;
PubMed=23186163; DOI=10.1021/pr300630k;
Zhou H., Di Palma S., Preisinger C., Peng M., Polat A.N., Heck A.J.,
Mohammed S.;
"Toward a comprehensive characterization of a human cancer cell
phosphoproteome.";
J. Proteome Res. 12:260-271(2013).
[32]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-442, AND IDENTIFICATION
BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
TISSUE=Liver;
PubMed=24275569; DOI=10.1016/j.jprot.2013.11.014;
Bian Y., Song C., Cheng K., Dong M., Wang F., Huang J., Sun D.,
Wang L., Ye M., Zou H.;
"An enzyme assisted RP-RPLC approach for in-depth analysis of human
liver phosphoproteome.";
J. Proteomics 96:253-262(2014).
[33]
FUNCTION, AND IDENTIFICATION IN THE EIF-3 COMPLEX.
PubMed=25849773; DOI=10.1038/nature14267;
Lee A.S., Kranzusch P.J., Cate J.H.;
"eIF3 targets cell-proliferation messenger RNAs for translational
activation or repression.";
Nature 522:111-114(2015).
[34]
IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
PubMed=25944712; DOI=10.1002/pmic.201400617;
Vaca Jacome A.S., Rabilloud T., Schaeffer-Reiss C., Rompais M.,
Ayoub D., Lane L., Bairoch A., Van Dorsselaer A., Carapito C.;
"N-terminome analysis of the human mitochondrial proteome.";
Proteomics 15:2519-2524(2015).
[35]
FUNCTION.
PubMed=27462815; DOI=10.1038/nature18954;
Lee A.S., Kranzusch P.J., Doudna J.A., Cate J.H.;
"eIF3d is an mRNA cap-binding protein that is required for specialized
translation initiation.";
Nature 536:96-99(2016).
[36]
3D-STRUCTURE MODELING, AND ELECTRON MICROSCOPY.
PubMed=16322461; DOI=10.1126/science.1118977;
Siridechadilok B., Fraser C.S., Hall R.J., Doudna J.A., Nogales E.;
"Structural roles for human translation factor eIF3 in initiation of
protein synthesis.";
Science 310:1513-1515(2005).
-!- FUNCTION: Component of the eukaryotic translation initiation
factor 3 (eIF-3) complex, which is required for several steps in
the initiation of protein synthesis (PubMed:17581632,
PubMed:25849773, PubMed:27462815). The eIF-3 complex associates
with the 40S ribosome and facilitates the recruitment of eIF-1,
eIF-1A, eIF-2:GTP:methionyl-tRNAi and eIF-5 to form the 43S pre-
initiation complex (43S PIC). The eIF-3 complex stimulates mRNA
recruitment to the 43S PIC and scanning of the mRNA for AUG
recognition. The eIF-3 complex is also required for disassembly
and recycling of post-termination ribosomal complexes and
subsequently prevents premature joining of the 40S and 60S
ribosomal subunits prior to initiation (PubMed:17581632). The eIF-
3 complex specifically targets and initiates translation of a
subset of mRNAs involved in cell proliferation, including cell
cycling, differentiation and apoptosis, and uses different modes
of RNA stem-loop binding to exert either translational activation
or repression (PubMed:25849773). Required for nonsense-mediated
mRNA decay (NMD); may act in conjunction with UPF2 to divert mRNAs
from translation to the NMD pathway (PubMed:17468741). May
interact with MCM7 and EPAS1 and regulate the proteasome-mediated
degradation of these proteins (PubMed:17310990, PubMed:17324924).
{ECO:0000255|HAMAP-Rule:MF_03004, ECO:0000269|PubMed:17310990,
ECO:0000269|PubMed:17324924, ECO:0000269|PubMed:17468741,
ECO:0000269|PubMed:17581632, ECO:0000269|PubMed:25849773,
ECO:0000269|PubMed:27462815}.
-!- SUBUNIT: Component of the eukaryotic translation initiation factor
3 (eIF-3) complex, which is composed of 13 subunits: EIF3A, EIF3B,
EIF3C, EIF3D, EIF3E, EIF3F, EIF3G, EIF3H, EIF3I, EIF3J, EIF3K,
EIF3L and EIF3M. The eIF-3 complex appears to include 3 stable
modules: module A is composed of EIF3A, EIF3B, EIF3G and EIF3I;
module B is composed of EIF3F, EIF3H, and EIF3M; and module C is
composed of EIF3C, EIF3D, EIF3E, EIF3K and EIF3L. EIF3C of module
C binds EIF3B of module A and EIF3H of module B, thereby linking
the three modules. EIF3J is a labile subunit that binds to the
eIF-3 complex via EIF3B. The eIF-3 complex interacts with RPS6KB1
under conditions of nutrient depletion. Mitogenic stimulation
leads to binding and activation of a complex composed of MTOR and
RPTOR, leading to phosphorylation and release of RPS6KB1 and
binding of EIF4B to eIF-3. Interacts with COPS3, COPS6, COPS7
(COPS7A or COPS7B), EIF4G1, EPAS1, MCM7, NCBP1, PSMC6, TRIM27 and
UPF2. Interacts with the HTLV-1 protein Tax-1. Interacts with
IFIT1 and IFIT2. {ECO:0000255|HAMAP-Rule:MF_03004,
ECO:0000269|PubMed:10504338, ECO:0000269|PubMed:11457827,
ECO:0000269|PubMed:11590142, ECO:0000269|PubMed:12220626,
ECO:0000269|PubMed:12386384, ECO:0000269|PubMed:16023166,
ECO:0000269|PubMed:16766523, ECO:0000269|PubMed:16973618,
ECO:0000269|PubMed:17310990, ECO:0000269|PubMed:17322308,
ECO:0000269|PubMed:17324924, ECO:0000269|PubMed:17468741,
ECO:0000269|PubMed:18599441, ECO:0000269|PubMed:25849773,
ECO:0000269|PubMed:8688078, ECO:0000269|PubMed:9295280}.
-!- INTERACTION:
Q8IY42:C4orf19; NbExp=3; IntAct=EBI-347740, EBI-10216552;
P55884:EIF3B; NbExp=6; IntAct=EBI-347740, EBI-366696;
Q99613:EIF3C; NbExp=13; IntAct=EBI-347740, EBI-353741;
O15371:EIF3D; NbExp=5; IntAct=EBI-347740, EBI-353818;
Q9UBQ5:EIF3K; NbExp=5; IntAct=EBI-347740, EBI-354344;
Q9Y262:EIF3L; NbExp=6; IntAct=EBI-347740, EBI-373519;
Q99814:EPAS1; NbExp=10; IntAct=EBI-347740, EBI-447470;
Q9Q2G4:ORF (xeno); NbExp=5; IntAct=EBI-347740, EBI-6248094;
Q59EK9:RUNDC3A; NbExp=4; IntAct=EBI-347740, EBI-747225;
P14373:TRIM27; NbExp=7; IntAct=EBI-347740, EBI-719493;
Q8IUH5:ZDHHC17; NbExp=2; IntAct=EBI-347740, EBI-524753;
-!- SUBCELLULAR LOCATION: Cytoplasm. Nucleus, PML body.
-!- TISSUE SPECIFICITY: Ubiquitously expressed. Expressed at highest
levels in appendix, lymph, pancreas, skeletal muscle, spleen and
thymus. {ECO:0000269|PubMed:8688078, ECO:0000269|PubMed:9295280}.
-!- MASS SPECTROMETRY: Mass=52131.8; Method=Unknown; Range=1-445;
Evidence={ECO:0000269|PubMed:17322308};
-!- MASS SPECTROMETRY: Mass=52133.4; Mass_error=0.2; Method=MALDI;
Range=1-445; Evidence={ECO:0000269|PubMed:18599441};
-!- SIMILARITY: Belongs to the eIF-3 subunit E family.
{ECO:0000255|HAMAP-Rule:MF_03004}.
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EMBL; U54562; AAC51760.1; -; mRNA.
EMBL; U94174; AAC51917.1; -; Genomic_DNA.
EMBL; U94162; AAC51917.1; JOINED; Genomic_DNA.
EMBL; U94163; AAC51917.1; JOINED; Genomic_DNA.
EMBL; U94164; AAC51917.1; JOINED; Genomic_DNA.
EMBL; U94165; AAC51917.1; JOINED; Genomic_DNA.
EMBL; U94166; AAC51917.1; JOINED; Genomic_DNA.
EMBL; U94167; AAC51917.1; JOINED; Genomic_DNA.
EMBL; U94168; AAC51917.1; JOINED; Genomic_DNA.
EMBL; U94169; AAC51917.1; JOINED; Genomic_DNA.
EMBL; U94170; AAC51917.1; JOINED; Genomic_DNA.
EMBL; U94171; AAC51917.1; JOINED; Genomic_DNA.
EMBL; U94172; AAC51917.1; JOINED; Genomic_DNA.
EMBL; U94173; AAC51917.1; JOINED; Genomic_DNA.
EMBL; U94175; AAC51919.1; -; mRNA.
EMBL; U62962; AAB58251.1; -; mRNA.
EMBL; U85947; AAB88873.1; -; mRNA.
EMBL; CR542275; CAG47071.1; -; mRNA.
EMBL; CH471060; EAW91918.1; -; Genomic_DNA.
EMBL; BC000734; AAH00734.1; -; mRNA.
EMBL; BC008419; AAH08419.1; -; mRNA.
EMBL; BC016706; AAH16706.1; -; mRNA.
EMBL; BC017887; AAH17887.1; -; mRNA.
EMBL; BC021679; AAH21679.1; -; mRNA.
CCDS; CCDS6308.1; -.
RefSeq; NP_001559.1; NM_001568.2.
UniGene; Hs.405590; -.
PDB; 3J8B; EM; -; E=1-395.
PDB; 3J8C; EM; -; E=1-395.
PDB; 6FEC; EM; 6.30 A; 3=1-445.
PDBsum; 3J8B; -.
PDBsum; 3J8C; -.
PDBsum; 6FEC; -.
ProteinModelPortal; P60228; -.
BioGrid; 109857; 108.
CORUM; P60228; -.
DIP; DIP-32691N; -.
IntAct; P60228; 60.
MINT; P60228; -.
STRING; 9606.ENSP00000220849; -.
iPTMnet; P60228; -.
PhosphoSitePlus; P60228; -.
SwissPalm; P60228; -.
BioMuta; EIF3E; -.
DMDM; 41019126; -.
EPD; P60228; -.
MaxQB; P60228; -.
PaxDb; P60228; -.
PeptideAtlas; P60228; -.
PRIDE; P60228; -.
ProteomicsDB; 57190; -.
DNASU; 3646; -.
Ensembl; ENST00000220849; ENSP00000220849; ENSG00000104408.
GeneID; 3646; -.
KEGG; hsa:3646; -.
UCSC; uc003ymu.4; human.
CTD; 3646; -.
DisGeNET; 3646; -.
EuPathDB; HostDB:ENSG00000104408.9; -.
GeneCards; EIF3E; -.
HGNC; HGNC:3277; EIF3E.
HPA; HPA023973; -.
MIM; 602210; gene.
neXtProt; NX_P60228; -.
OpenTargets; ENSG00000104408; -.
PharmGKB; PA27705; -.
eggNOG; KOG2758; Eukaryota.
eggNOG; ENOG410XQK5; LUCA.
GeneTree; ENSGT00390000002661; -.
HOVERGEN; HBG001097; -.
InParanoid; P60228; -.
KO; K03250; -.
OMA; GFFRTQV; -.
OrthoDB; EOG091G075K; -.
PhylomeDB; P60228; -.
TreeFam; TF101518; -.
Reactome; R-HSA-156827; L13a-mediated translational silencing of Ceruloplasmin expression.
Reactome; R-HSA-72649; Translation initiation complex formation.
Reactome; R-HSA-72689; Formation of a pool of free 40S subunits.
Reactome; R-HSA-72695; Formation of the ternary complex, and subsequently, the 43S complex.
Reactome; R-HSA-72702; Ribosomal scanning and start codon recognition.
Reactome; R-HSA-72706; GTP hydrolysis and joining of the 60S ribosomal subunit.
ChiTaRS; EIF3E; human.
GeneWiki; EIF3S6; -.
GenomeRNAi; 3646; -.
PRO; PR:P60228; -.
Proteomes; UP000005640; Chromosome 8.
Bgee; ENSG00000104408; Expressed in 236 organ(s), highest expression level in epithelium of mammary gland.
CleanEx; HS_EIF3E; -.
ExpressionAtlas; P60228; baseline and differential.
Genevisible; P60228; HS.
GO; GO:0005737; C:cytoplasm; IDA:UniProtKB.
GO; GO:0005829; C:cytosol; IDA:HPA.
GO; GO:0005852; C:eukaryotic translation initiation factor 3 complex; IDA:UniProtKB.
GO; GO:0070062; C:extracellular exosome; HDA:UniProtKB.
GO; GO:0016020; C:membrane; HDA:UniProtKB.
GO; GO:0016604; C:nuclear body; IDA:HPA.
GO; GO:0005654; C:nucleoplasm; NAS:UniProtKB.
GO; GO:0005634; C:nucleus; IDA:UniProtKB.
GO; GO:0016605; C:PML body; IEA:UniProtKB-SubCell.
GO; GO:0045296; F:cadherin binding; HDA:BHF-UCL.
GO; GO:0047485; F:protein N-terminus binding; IPI:UniProtKB.
GO; GO:0003723; F:RNA binding; HDA:UniProtKB.
GO; GO:0003743; F:translation initiation factor activity; IC:UniProtKB.
GO; GO:0045947; P:negative regulation of translational initiation; NAS:UniProtKB.
GO; GO:0000184; P:nuclear-transcribed mRNA catabolic process, nonsense-mediated decay; IMP:UniProtKB.
GO; GO:1902416; P:positive regulation of mRNA binding; IPI:ParkinsonsUK-UCL.
GO; GO:0045727; P:positive regulation of translation; IPI:ParkinsonsUK-UCL.
GO; GO:0006446; P:regulation of translational initiation; NAS:UniProtKB.
GO; GO:0006413; P:translational initiation; IDA:UniProtKB.
Gene3D; 1.10.10.10; -; 1.
HAMAP; MF_03004; eIF3e; 1.
InterPro; IPR016650; eIF3e.
InterPro; IPR019010; eIF3e_N.
InterPro; IPR000717; PCI_dom.
InterPro; IPR036388; WH-like_DNA-bd_sf.
InterPro; IPR036390; WH_DNA-bd_sf.
PANTHER; PTHR10317; PTHR10317; 1.
Pfam; PF09440; eIF3_N; 1.
Pfam; PF01399; PCI; 1.
PIRSF; PIRSF016255; eIF3e_su6; 1.
SMART; SM01186; eIF3_N; 1.
SMART; SM00088; PINT; 1.
SUPFAM; SSF46785; SSF46785; 1.
PROSITE; PS50250; PCI; 1.
1: Evidence at protein level;
3D-structure; Acetylation; Complete proteome; Cytoplasm;
Direct protein sequencing; Initiation factor; Nucleus; Phosphoprotein;
Polymorphism; Protein biosynthesis; Reference proteome.
INIT_MET 1 1 Removed. {ECO:0000244|PubMed:19413330,
ECO:0000244|PubMed:22223895,
ECO:0000244|PubMed:22814378,
ECO:0000255|HAMAP-Rule:MF_03004,
ECO:0000269|PubMed:17322308,
ECO:0000269|Ref.8}.
CHAIN 2 445 Eukaryotic translation initiation factor
3 subunit E.
/FTId=PRO_0000123515.
DOMAIN 221 398 PCI. {ECO:0000255|PROSITE-
ProRule:PRU01185}.
REGION 4 128 Sufficient for interaction with EPAS1.
{ECO:0000269|PubMed:17324924}.
REGION 9 195 Sufficient for interaction with TRIM27.
{ECO:0000269|PubMed:10504338}.
REGION 351 445 Sufficient for interaction with MCM7.
{ECO:0000269|PubMed:17310990}.
MOD_RES 2 2 N-acetylalanine.
{ECO:0000244|PubMed:19413330,
ECO:0000244|PubMed:22223895,
ECO:0000244|PubMed:22814378,
ECO:0000255|HAMAP-Rule:MF_03004,
ECO:0000269|PubMed:17322308,
ECO:0000269|Ref.8}.
MOD_RES 399 399 Phosphoserine.
{ECO:0000244|PubMed:18669648,
ECO:0000244|PubMed:20068231,
ECO:0000244|PubMed:23186163}.
MOD_RES 439 439 Phosphothreonine.
{ECO:0000250|UniProtKB:P60229}.
MOD_RES 442 442 Phosphoserine.
{ECO:0000244|PubMed:24275569}.
MOD_RES 445 445 Phosphotyrosine.
{ECO:0000250|UniProtKB:P60229}.
VARIANT 185 185 A -> V (in dbSNP:rs17856554).
{ECO:0000269|PubMed:15489334}.
/FTId=VAR_046480.
MUTAGEN 312 312 L->D: Promotes nuclear accumulation.
{ECO:0000269|PubMed:17761670}.
HELIX 6 12 {ECO:0000244|PDB:3J8B}.
HELIX 16 19 {ECO:0000244|PDB:3J8B}.
HELIX 21 29 {ECO:0000244|PDB:3J8B}.
HELIX 35 45 {ECO:0000244|PDB:3J8B}.
HELIX 51 58 {ECO:0000244|PDB:3J8B}.
HELIX 67 92 {ECO:0000244|PDB:3J8B}.
HELIX 124 140 {ECO:0000244|PDB:3J8B}.
HELIX 144 152 {ECO:0000244|PDB:3J8B}.
HELIX 161 165 {ECO:0000244|PDB:3J8B}.
HELIX 166 179 {ECO:0000244|PDB:3J8B}.
HELIX 182 194 {ECO:0000244|PDB:3J8B}.
STRAND 200 202 {ECO:0000244|PDB:3J8B}.
HELIX 205 218 {ECO:0000244|PDB:3J8B}.
HELIX 232 236 {ECO:0000244|PDB:3J8B}.
STRAND 246 248 {ECO:0000244|PDB:3J8B}.
HELIX 250 262 {ECO:0000244|PDB:3J8B}.
TURN 265 267 {ECO:0000244|PDB:3J8B}.
HELIX 270 273 {ECO:0000244|PDB:3J8B}.
HELIX 274 278 {ECO:0000244|PDB:3J8B}.
HELIX 281 289 {ECO:0000244|PDB:3J8B}.
HELIX 291 301 {ECO:0000244|PDB:3J8B}.
HELIX 305 319 {ECO:0000244|PDB:3J8B}.
TURN 323 325 {ECO:0000244|PDB:3J8B}.
HELIX 326 328 {ECO:0000244|PDB:3J8B}.
HELIX 329 347 {ECO:0000244|PDB:3J8B}.
STRAND 349 352 {ECO:0000244|PDB:3J8B}.
HELIX 353 359 {ECO:0000244|PDB:3J8B}.
STRAND 360 362 {ECO:0000244|PDB:3J8B}.
HELIX 364 376 {ECO:0000244|PDB:3J8B}.
TURN 386 389 {ECO:0000244|PDB:3J8B}.
STRAND 390 392 {ECO:0000244|PDB:3J8B}.
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


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