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Eukaryotic translation initiation factor 4E (eIF-4E) (eIF4E) (eIF-4F 25 kDa subunit) (mRNA cap-binding protein)

 IF4E_HUMAN              Reviewed;         217 AA.
P06730; B7Z6V1; D6RCQ6; Q96E95;
01-JAN-1988, integrated into UniProtKB/Swiss-Prot.
01-FEB-1996, sequence version 2.
25-OCT-2017, entry version 199.
RecName: Full=Eukaryotic translation initiation factor 4E;
Short=eIF-4E;
Short=eIF4E;
AltName: Full=eIF-4F 25 kDa subunit;
AltName: Full=mRNA cap-binding protein;
Name=EIF4E; Synonyms=EIF4EL1, EIF4F;
Homo sapiens (Human).
Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
Catarrhini; Hominidae; Homo.
NCBI_TaxID=9606;
[1]
NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1).
TISSUE=Placenta;
PubMed=3469651; DOI=10.1073/pnas.84.4.945;
Rychlik W., Domier L.L., Gardner P.R., Hellmann G.M., Rhoads R.E.;
"Amino acid sequence of the mRNA cap-binding protein from human
tissues.";
Proc. Natl. Acad. Sci. U.S.A. 84:945-949(1987).
[2]
ERRATUM, AND SEQUENCE REVISION TO 108 AND 189.
PubMed=1736299; DOI=10.1073/pnas.89.3.1148-c;
Rychlik W., Domier L.L., Gardner P.R., Hellmann G.M., Rhoads R.E.;
Proc. Natl. Acad. Sci. U.S.A. 89:1148-1148(1992).
[3]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 3).
TISSUE=Small intestine;
PubMed=14702039; DOI=10.1038/ng1285;
Ota T., Suzuki Y., Nishikawa T., Otsuki T., Sugiyama T., Irie R.,
Wakamatsu A., Hayashi K., Sato H., Nagai K., Kimura K., Makita H.,
Sekine M., Obayashi M., Nishi T., Shibahara T., Tanaka T., Ishii S.,
Yamamoto J., Saito K., Kawai Y., Isono Y., Nakamura Y., Nagahari K.,
Murakami K., Yasuda T., Iwayanagi T., Wagatsuma M., Shiratori A.,
Sudo H., Hosoiri T., Kaku Y., Kodaira H., Kondo H., Sugawara M.,
Takahashi M., Kanda K., Yokoi T., Furuya T., Kikkawa E., Omura Y.,
Abe K., Kamihara K., Katsuta N., Sato K., Tanikawa M., Yamazaki M.,
Ninomiya K., Ishibashi T., Yamashita H., Murakawa K., Fujimori K.,
Tanai H., Kimata M., Watanabe M., Hiraoka S., Chiba Y., Ishida S.,
Ono Y., Takiguchi S., Watanabe S., Yosida M., Hotuta T., Kusano J.,
Kanehori K., Takahashi-Fujii A., Hara H., Tanase T.-O., Nomura Y.,
Togiya S., Komai F., Hara R., Takeuchi K., Arita M., Imose N.,
Musashino K., Yuuki H., Oshima A., Sasaki N., Aotsuka S.,
Yoshikawa Y., Matsunawa H., Ichihara T., Shiohata N., Sano S.,
Moriya S., Momiyama H., Satoh N., Takami S., Terashima Y., Suzuki O.,
Nakagawa S., Senoh A., Mizoguchi H., Goto Y., Shimizu F., Wakebe H.,
Hishigaki H., Watanabe T., Sugiyama A., Takemoto M., Kawakami B.,
Yamazaki M., Watanabe K., Kumagai A., Itakura S., Fukuzumi Y.,
Fujimori Y., Komiyama M., Tashiro H., Tanigami A., Fujiwara T.,
Ono T., Yamada K., Fujii Y., Ozaki K., Hirao M., Ohmori Y.,
Kawabata A., Hikiji T., Kobatake N., Inagaki H., Ikema Y., Okamoto S.,
Okitani R., Kawakami T., Noguchi S., Itoh T., Shigeta K., Senba T.,
Matsumura K., Nakajima Y., Mizuno T., Morinaga M., Sasaki M.,
Togashi T., Oyama M., Hata H., Watanabe M., Komatsu T.,
Mizushima-Sugano J., Satoh T., Shirai Y., Takahashi Y., Nakagawa K.,
Okumura K., Nagase T., Nomura N., Kikuchi H., Masuho Y., Yamashita R.,
Nakai K., Yada T., Nakamura Y., Ohara O., Isogai T., Sugano S.;
"Complete sequencing and characterization of 21,243 full-length human
cDNAs.";
Nat. Genet. 36:40-45(2004).
[4]
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
PubMed=15815621; DOI=10.1038/nature03466;
Hillier L.W., Graves T.A., Fulton R.S., Fulton L.A., Pepin K.H.,
Minx P., Wagner-McPherson C., Layman D., Wylie K., Sekhon M.,
Becker M.C., Fewell G.A., Delehaunty K.D., Miner T.L., Nash W.E.,
Kremitzki C., Oddy L., Du H., Sun H., Bradshaw-Cordum H., Ali J.,
Carter J., Cordes M., Harris A., Isak A., van Brunt A., Nguyen C.,
Du F., Courtney L., Kalicki J., Ozersky P., Abbott S., Armstrong J.,
Belter E.A., Caruso L., Cedroni M., Cotton M., Davidson T., Desai A.,
Elliott G., Erb T., Fronick C., Gaige T., Haakenson W., Haglund K.,
Holmes A., Harkins R., Kim K., Kruchowski S.S., Strong C.M.,
Grewal N., Goyea E., Hou S., Levy A., Martinka S., Mead K.,
McLellan M.D., Meyer R., Randall-Maher J., Tomlinson C.,
Dauphin-Kohlberg S., Kozlowicz-Reilly A., Shah N.,
Swearengen-Shahid S., Snider J., Strong J.T., Thompson J., Yoakum M.,
Leonard S., Pearman C., Trani L., Radionenko M., Waligorski J.E.,
Wang C., Rock S.M., Tin-Wollam A.-M., Maupin R., Latreille P.,
Wendl M.C., Yang S.-P., Pohl C., Wallis J.W., Spieth J., Bieri T.A.,
Berkowicz N., Nelson J.O., Osborne J., Ding L., Meyer R., Sabo A.,
Shotland Y., Sinha P., Wohldmann P.E., Cook L.L., Hickenbotham M.T.,
Eldred J., Williams D., Jones T.A., She X., Ciccarelli F.D.,
Izaurralde E., Taylor J., Schmutz J., Myers R.M., Cox D.R., Huang X.,
McPherson J.D., Mardis E.R., Clifton S.W., Warren W.C.,
Chinwalla A.T., Eddy S.R., Marra M.A., Ovcharenko I., Furey T.S.,
Miller W., Eichler E.E., Bork P., Suyama M., Torrents D.,
Waterston R.H., Wilson R.K.;
"Generation and annotation of the DNA sequences of human chromosomes 2
and 4.";
Nature 434:724-731(2005).
[5]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
TISSUE=Brain, and Testis;
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).
[6]
NUCLEOTIDE SEQUENCE [MRNA] OF 1-214 (ISOFORM 2).
TISSUE=Myeloma;
PubMed=16341674; DOI=10.1007/s00335-005-0075-2;
Oh J.H., Yang J.O., Hahn Y., Kim M.R., Byun S.S., Jeon Y.J., Kim J.M.,
Song K.S., Noh S.M., Kim S., Yoo H.S., Kim Y.S., Kim N.S.;
"Transcriptome analysis of human gastric cancer.";
Mamm. Genome 16:942-954(2005).
[7]
PARTIAL PROTEIN SEQUENCE.
PubMed=1993647;
Marino M.W., Feld L.J., Jaffe E.A., Pfeffer L.M., Han Y.-M.,
Donner D.B.;
"Phosphorylation of the proto-oncogene product eukaryotic initiation
factor 4E is a common cellular response to tumor necrosis factor.";
J. Biol. Chem. 266:2685-2688(1991).
[8]
MUTAGENESIS OF TRP-102; GLU-103; ASP-104 AND GLU-105.
PubMed=1672854; DOI=10.1016/0014-5793(91)80294-D;
Ueda H., Iyo H., Doi M., Inoue M., Ishida T., Morioka H., Tanaka T.,
Nishikawa S., Uesugi S.;
"Combination of Trp and Glu residues for recognition of mRNA cap
structure. Analysis of m7G base recognition site of human cap binding
protein (IF-4E) by site-directed mutagenesis.";
FEBS Lett. 280:207-210(1991).
[9]
PHOSPHORYLATION.
PubMed=3112145;
Rychlik W., Russ M.A., Rhoads R.E.;
"Phosphorylation site of eukaryotic initiation factor 4E.";
J. Biol. Chem. 262:10434-10437(1987).
[10]
PHOSPHORYLATION, AND MUTAGENESIS OF SER-53.
PubMed=8505316;
Kaufman R.J., Murtha-Riel P., Pittman D.D., Davies M.V.;
"Characterization of wild-type and Ser53 mutant eukaryotic initiation
factor 4E overexpression in mammalian cells.";
J. Biol. Chem. 268:11902-11909(1993).
[11]
PHOSPHORYLATION, AND MUTAGENESIS OF SER-53.
PubMed=7590282; DOI=10.1016/0378-1119(95)00302-M;
Zhang Y., Klein H.L., Schneider R.J.;
"Role of Ser-53 phosphorylation in the activity of human translation
initiation factor eIF-4E in mammalian and yeast cells.";
Gene 163:283-288(1995).
[12]
PHOSPHORYLATION AT SER-209.
PubMed=7782323; DOI=10.1074/jbc.270.24.14597;
Joshi B., Cai A.L., Keiper B.D., Minich W.B., Mendez R., Beach C.M.,
Stepinski J., Stolarski R., Darzynkiewicz E., Rhoads R.E.;
"Phosphorylation of eukaryotic protein synthesis initiation factor 4E
at Ser-209.";
J. Biol. Chem. 270:14597-14603(1995).
[13]
PHOSPHORYLATION AT SER-209.
PubMed=7665584; DOI=10.1074/jbc.270.37.21684;
Flynn A., Proud C.G.;
"Serine 209, not serine 53, is the major site of phosphorylation in
initiation factor eIF-4E in serum-treated Chinese hamster ovary
cells.";
J. Biol. Chem. 270:21684-21688(1995).
[14]
INTERACTION WITH EIF4G AND EIF4EBP1.
PubMed=8521827;
Haghighat A., Mader S., Pause A., Sonenberg N.;
"Repression of cap-dependent translation by 4E-binding protein 1:
competition with p220 for binding to eukaryotic initiation factor-
4E.";
EMBO J. 14:5701-5709(1995).
[15]
INTERACTION WITH EIF4ENIF1.
TISSUE=Fetal brain, and Placenta;
PubMed=10856257; DOI=10.1093/emboj/19.12.3142;
Dostie J., Ferraiuolo M., Pause A., Adam S.A., Sonenberg N.;
"A novel shuttling protein, 4E-T, mediates the nuclear import of the
mRNA 5' cap-binding protein, eIF4E.";
EMBO J. 19:3142-3156(2000).
[16]
PHOSPHORYLATION BY MKNK1.
PubMed=9878069; DOI=10.1093/emboj/18.1.270;
Pyronnet S., Imataka H., Gingras A.-C., Fukunaga R., Hunter T.,
Sonenberg N.;
"Human eukaryotic translation initiation factor 4G (eIF4G) recruits
mnk1 to phosphorylate eIF4E.";
EMBO J. 18:270-279(1999).
[17]
INTERACTION WITH EIF4A1 AND EIF4A2.
PubMed=11408474; DOI=10.1074/jbc.C100284200;
Li W., Belsham G.J., Proud C.G.;
"Eukaryotic initiation factors 4A (eIF4A) and 4G (eIF4G) mutually
interact in a 1:1 ratio in vivo.";
J. Biol. Chem. 276:29111-29115(2001).
[18]
PHOSPHORYLATION AT SER-209 BY MKNK2.
PubMed=11154262; DOI=10.1128/MCB.21.3.743-754.2001;
Scheper G.C., Morrice N.A., Kleijn M., Proud C.G.;
"The mitogen-activated protein kinase signal-integrating kinase Mnk2
is a eukaryotic initiation factor 4E kinase with high levels of basal
activity in mammalian cells.";
Mol. Cell. Biol. 21:743-754(2001).
[19]
INTERACTION WITH MKNK2.
PubMed=12897141; DOI=10.1128/MCB.23.16.5692-5705.2003;
Scheper G.C., Parra J.L., Wilson M., Van Kollenburg B.,
Vertegaal A.C.O., Han Z.-G., Proud C.G.;
"The N and C termini of the splice variants of the human mitogen-
activated protein kinase-interacting kinase Mnk2 determine activity
and localization.";
Mol. Cell. Biol. 23:5692-5705(2003).
[20]
INTERACTION WITH APOBEC3G.
PubMed=16699599; DOI=10.1371/journal.ppat.0020041;
Wichroski M.J., Robb G.B., Rana T.M.;
"Human retroviral host restriction factors APOBEC3G and APOBEC3F
localize to mRNA processing bodies.";
PLoS Pathog. 2:E41-E41(2006).
[21]
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).
[22]
INVOLVEMENT IN AUTS19, AND CHROMOSOMAL TRANSLOCATION.
PubMed=19556253; DOI=10.1136/jmg.2009.066852;
Neves-Pereira M., Mueller B., Massie D., Williams J.H., O'Brien P.C.,
Hughes A., Shen S.B., Clair D.S., Miedzybrodzka Z.;
"Deregulation of EIF4E: a novel mechanism for autism.";
J. Med. Genet. 46:759-765(2009).
[23]
INTERACTION WITH LARP1.
PubMed=20430826; DOI=10.1093/nar/gkq294;
Burrows C., Abd Latip N., Lam S.J., Carpenter L., Sawicka K.,
Tzolovsky G., Gabra H., Bushell M., Glover D.M., Willis A.E.,
Blagden S.P.;
"The RNA binding protein Larp1 regulates cell division, apoptosis and
cell migration.";
Nucleic Acids Res. 38:5542-5553(2010).
[24]
SUBCELLULAR LOCATION, AND INTERACTION WITH LIMD1; WTIP AND AJUBA.
PubMed=20616046; DOI=10.1073/pnas.0914987107;
James V., Zhang Y., Foxler D.E., de Moor C.H., Kong Y.W., Webb T.M.,
Self T.J., Feng Y., Lagos D., Chu C.Y., Rana T.M., Morley S.J.,
Longmore G.D., Bushell M., Sharp T.V.;
"LIM-domain proteins, LIMD1, Ajuba, and WTIP are required for
microRNA-mediated gene silencing.";
Proc. Natl. Acad. Sci. U.S.A. 107:12499-12504(2010).
[25]
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).
[26]
FUNCTION, AND MUTAGENESIS OF TRP-73.
PubMed=22578813; DOI=10.1016/j.molcel.2012.04.004;
Yanagiya A., Suyama E., Adachi H., Svitkin Y.V., Aza-Blanc P.,
Imataka H., Mikami S., Martineau Y., Ronai Z.A., Sonenberg N.;
"Translational homeostasis via the mRNA cap-binding protein, eIF4E.";
Mol. Cell 46:847-858(2012).
[27]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-22, AND IDENTIFICATION
BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
TISSUE=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).
[28]
INTERACTION WITH EIF4EBP2.
PubMed=24207126; DOI=10.1016/j.str.2013.08.030;
Lukhele S., Bah A., Lin H., Sonenberg N., Forman-Kay J.D.;
"Interaction of the eukaryotic initiation factor 4E with 4E-BP2 at a
dynamic bipartite interface.";
Structure 21:2186-2196(2013).
[29]
INTERACTION WITH EIF4EBP2.
PubMed=25533957; DOI=10.1038/nature13999;
Bah A., Vernon R.M., Siddiqui Z., Krzeminski M., Muhandiram R.,
Zhao C., Sonenberg N., Kay L.E., Forman-Kay J.D.;
"Folding of an intrinsically disordered protein by phosphorylation as
a regulatory switch.";
Nature 519:106-109(2015).
[30]
INTERACTION WITH METTL3.
PubMed=27117702; DOI=10.1016/j.molcel.2016.03.021;
Lin S., Choe J., Du P., Triboulet R., Gregory R.I.;
"The m(6)A methyltransferase METTL3 promotes translation in human
cancer cells.";
Mol. Cell 62:335-345(2016).
[31]
X-RAY CRYSTALLOGRAPHY (2.0 ANGSTROMS) IN COMPLEX WITH MRNA CAP
ANALOGS.
PubMed=11879179; DOI=10.1042/0264-6021:3620539;
Tomoo K., Shen X., Okabe K., Nozoe Y., Fukuhara S., Morino S.,
Ishida T., Taniguchi T., Hasegawa H., Terashima A., Sasaki M.,
Katsuya Y., Kitamura K., Miyoshi H., Ishikawa M., Miura K.;
"Crystal structures of 7-methylguanosine 5'-triphosphate
(m(7)GTP)- and P(1)-7-methylguanosine-P(3)-adenosine-5',5'-
triphosphate (m(7)GpppA)-bound human full-length eukaryotic initiation
factor 4E: biological importance of the C-terminal flexible region.";
Biochem. J. 362:539-544(2002).
[32]
STRUCTURE BY NMR IN COMPLEX WITH EIF4G3 AND MRNA CAP ANALOGS.
PubMed=12975586; DOI=10.1023/A:1025442322316;
Miura T., Shiratori Y., Shimma N.;
"Backbone resonance assignment of human eukaryotic translation
initiation factor 4E (eIF4E) in complex with 7-methylguanosine
diphosphate (m7GDP) and a 17-amino acid peptide derived from human
eIF4GII.";
J. Biomol. NMR 27:279-280(2003).
[33]
X-RAY CRYSTALLOGRAPHY (2.10 ANGSTROMS) OF 27-217 IN COMPLEX WITH MRNA
CAP ANALOG AND EIF4EBP1, FUNCTION, AND INTERACTION WITH EIF4EBP1;
EIF4EBP2 AND EIF4EBP3.
PubMed=16271312; DOI=10.1016/j.bbapap.2005.07.023;
Tomoo K., Matsushita Y., Fujisaki H., Abiko F., Shen X., Taniguchi T.,
Miyagawa H., Kitamura K., Miura K., Ishida T.;
"Structural basis for mRNA cap-binding regulation of eukaryotic
initiation factor 4E by 4E-binding protein, studied by spectroscopic,
X-ray crystal structural, and molecular dynamics simulation methods.";
Biochim. Biophys. Acta 1753:191-208(2005).
[34]
STRUCTURE BY NMR, CLEAVAGE OF INITIATOR METHIONINE, MASS SPECTROMETRY,
AND MUTAGENESIS OF LYS-119.
PubMed=17036047; DOI=10.1038/sj.emboj.7601380;
Volpon L., Osborne M.J., Topisirovic I., Siddiqui N., Borden K.L.B.;
"Cap-free structure of eIF4E suggests a basis for conformational
regulation by its ligands.";
EMBO J. 25:5138-5149(2006).
[35]
X-RAY CRYSTALLOGRAPHY (2.10 ANGSTROMS) IN COMPLEX WITH MRNA CAP
ANALOGS, AND MASS SPECTROMETRY.
PubMed=17631896; DOI=10.1016/j.jmb.2007.06.033;
Brown C.J., McNae I., Fischer P.M., Walkinshaw M.D.;
"Crystallographic and mass spectrometric characterisation of eIF4E
with N7-alkylated cap derivatives.";
J. Mol. Biol. 372:7-15(2007).
[36]
X-RAY CRYSTALLOGRAPHY (2.2 ANGSTROMS) OF 27-217 IN COMPLEX WITH
EIF4EBP2, AND INTERACTION WITH EIF4EBP2.
PubMed=21661078; DOI=10.1002/psc.1384;
Fukuyo A., In Y., Ishida T., Tomoo K.;
"Structural scaffold for eIF4E binding selectivity of 4E-BP isoforms:
crystal structure of eIF4E binding region of 4E-BP2 and its comparison
with that of 4E-BP1.";
J. Pept. Sci. 17:650-657(2011).
-!- FUNCTION: Recognizes and binds the 7-methylguanosine-containing
mRNA cap during an early step in the initiation of protein
synthesis and facilitates ribosome binding by inducing the
unwinding of the mRNAs secondary structures. Component of the
CYFIP1-EIF4E-FMR1 complex which binds to the mRNA cap and mediates
translational repression. In the CYFIP1-EIF4E-FMR1 complex this
subunit mediates the binding to the mRNA cap.
{ECO:0000269|PubMed:16271312, ECO:0000269|PubMed:22578813}.
-!- SUBUNIT: eIF4F is a multi-subunit complex, the composition of
which varies with external and internal environmental conditions.
It is composed of at least EIF4A, EIF4E and EIF4G1/EIF4G3. EIF4E
is also known to interact with other partners. The interaction
with EIF4ENIF1 mediates the import into the nucleus.
Hypophosphorylated EIF4EBP1, EIF4EBP2 and EIF4EBP3 compete with
EIF4G1/EIF4G3 to interact with EIF4E; insulin stimulated MAP-
kinase (MAPK1 and MAPK3) phosphorylation of EIF4EBP1 causes
dissociation of the complex allowing EIF4G1/EIF4G3 to bind and
consequent initiation of translation (PubMed:24207126,
PubMed:25533957, PubMed:21661078). Rapamycin can attenuate insulin
stimulation, mediated by FKBPs. Interacts mutually exclusive with
EIF4A1 or EIF4A2. Interacts with NGDN and PIWIL2. Component of the
CYFIP1-EIF4E-FMR1 complex composed of CYFIP, EIF4E and FMR1.
Interacts directly with CYFIP1. Interacts with CLOCK (By
similarity). Interacts with Lassa virus Z protein. Binds to MKNK2
in nucleus. Interacts with LIMD1, WTIP and AJUBA. Interacts with
APOBEC3G in an RNA-dependent manner. Interacts with LARP1.
Interacts with METTL3 (PubMed:27117702).
{ECO:0000250|UniProtKB:P63073, ECO:0000269|PubMed:10856257,
ECO:0000269|PubMed:11408474, ECO:0000269|PubMed:11879179,
ECO:0000269|PubMed:12897141, ECO:0000269|PubMed:12975586,
ECO:0000269|PubMed:16271312, ECO:0000269|PubMed:16699599,
ECO:0000269|PubMed:17631896, ECO:0000269|PubMed:20430826,
ECO:0000269|PubMed:20616046, ECO:0000269|PubMed:21661078,
ECO:0000269|PubMed:24207126, ECO:0000269|PubMed:25533957,
ECO:0000269|PubMed:8521827}.
-!- INTERACTION:
O70552:Btg4 (xeno); NbExp=4; IntAct=EBI-73440, EBI-16204405;
Q60809:Cnot7 (xeno); NbExp=2; IntAct=EBI-73440, EBI-2104739;
Q13541:EIF4EBP1; NbExp=19; IntAct=EBI-73440, EBI-74090;
Q13542:EIF4EBP2; NbExp=8; IntAct=EBI-73440, EBI-935137;
O60516:EIF4EBP3; NbExp=5; IntAct=EBI-73440, EBI-746950;
Q9NRA8:EIF4ENIF1; NbExp=9; IntAct=EBI-73440, EBI-301024;
Q04637:EIF4G1; NbExp=9; IntAct=EBI-73440, EBI-73711;
O43432-1:EIF4G3; NbExp=2; IntAct=EBI-73440, EBI-15841003;
Q04743:EMX2; NbExp=4; IntAct=EBI-73440, EBI-399831;
Q8TEQ6:GEMIN5; NbExp=3; IntAct=EBI-73440, EBI-443630;
Q63ZY3:KANK2; NbExp=5; IntAct=EBI-73440, EBI-2556193;
P42704:LRPPRC; NbExp=6; IntAct=EBI-73440, EBI-1050853;
P11940:PABPC1; NbExp=5; IntAct=EBI-73440, EBI-81531;
P63165:SUMO1; NbExp=5; IntAct=EBI-73440, EBI-80140;
P48775:TDO2; NbExp=3; IntAct=EBI-73440, EBI-743494;
P14373:TRIM27; NbExp=3; IntAct=EBI-73440, EBI-719493;
Q5T124:UBXN11; NbExp=3; IntAct=EBI-73440, EBI-746004;
O73557:Z (xeno); NbExp=3; IntAct=EBI-73440, EBI-15840965;
-!- SUBCELLULAR LOCATION: Cytoplasm, P-body
{ECO:0000269|PubMed:20616046}. Cytoplasm {ECO:0000250}.
-!- ALTERNATIVE PRODUCTS:
Event=Alternative splicing; Named isoforms=3;
Name=1;
IsoId=P06730-1; Sequence=Displayed;
Name=2;
IsoId=P06730-2; Sequence=VSP_042014;
Note=No experimental confirmation available.;
Name=3;
IsoId=P06730-3; Sequence=VSP_043591;
Note=No experimental confirmation available.;
-!- PTM: Phosphorylation increases the ability of the protein to bind
to mRNA caps and to form the eIF4F complex.
{ECO:0000269|PubMed:11154262, ECO:0000269|PubMed:3112145,
ECO:0000269|PubMed:7590282, ECO:0000269|PubMed:7665584,
ECO:0000269|PubMed:7782323, ECO:0000269|PubMed:8505316,
ECO:0000269|PubMed:9878069}.
-!- MASS SPECTROMETRY: Mass=24964.3; Method=Electrospray; Range=2-217;
Evidence={ECO:0000269|PubMed:17036047};
-!- MASS SPECTROMETRY: Mass=24960; Method=Electrospray; Range=2-217;
Evidence={ECO:0000269|PubMed:17631896};
-!- DISEASE: Autism 19 (AUTS19) [MIM:615091]: A complex
multifactorial, pervasive developmental disorder characterized by
impairments in reciprocal social interaction and communication,
restricted and stereotyped patterns of interests and activities,
and the presence of developmental abnormalities by 3 years of age.
Most individuals with autism also manifest moderate mental
retardation. {ECO:0000269|PubMed:19556253}. Note=Disease
susceptibility is associated with variations affecting the gene
represented in this entry. A heterozygous single-nucleotide
insertion has been found in families affected by autism. The
variant results in increased promoter activity and is involved in
disease pathogenesis through EIF4E deregulation (PubMed:19556253).
{ECO:0000269|PubMed:19556253}.
-!- DISEASE: Note=A chromosomal aberration involving EIF4E has been
found in a patient with classic autism. Translocation
t(45)(q23q31.3). The breakpoint on chromosome 4 is located 56 kb
downstream of EIF4E (PubMed:19556253).
{ECO:0000269|PubMed:19556253}.
-!- SIMILARITY: Belongs to the eukaryotic initiation factor 4E family.
{ECO:0000305}.
-!- CAUTION: Was originally thought to be phosphorylated on Ser-53
(PubMed:3112145); this was later shown to be wrong
(PubMed:7665584). {ECO:0000305|PubMed:3112145,
ECO:0000305|PubMed:7665584}.
-!- WEB RESOURCE: Name=Atlas of Genetics and Cytogenetics in Oncology
and Haematology;
URL="http://atlasgeneticsoncology.org/Genes/EIF4EID40431ch4q23.html";
-----------------------------------------------------------------------
Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms
Distributed under the Creative Commons Attribution-NoDerivs License
-----------------------------------------------------------------------
EMBL; M15353; AAC13647.1; -; mRNA.
EMBL; AK300982; BAH13387.1; -; mRNA.
EMBL; AC019131; -; NOT_ANNOTATED_CDS; Genomic_DNA.
EMBL; AC093836; -; NOT_ANNOTATED_CDS; Genomic_DNA.
EMBL; BC012611; AAH12611.1; -; mRNA.
EMBL; BC035166; AAH35166.1; -; mRNA.
EMBL; BC043226; AAH43226.1; -; mRNA.
EMBL; BM849222; -; NOT_ANNOTATED_CDS; mRNA.
CCDS; CCDS34031.1; -. [P06730-1]
CCDS; CCDS47109.1; -. [P06730-3]
CCDS; CCDS54779.1; -. [P06730-2]
PIR; A26411; A26411.
RefSeq; NP_001124150.1; NM_001130678.2. [P06730-3]
RefSeq; NP_001124151.1; NM_001130679.2. [P06730-2]
RefSeq; NP_001317946.1; NM_001331017.1.
RefSeq; NP_001959.1; NM_001968.4. [P06730-1]
UniGene; Hs.13211; -.
UniGene; Hs.249718; -.
PDB; 1IPB; X-ray; 2.00 A; A=1-217.
PDB; 1IPC; X-ray; 2.00 A; A=1-217.
PDB; 1WKW; X-ray; 2.10 A; A=27-217.
PDB; 2GPQ; NMR; -; A=1-217.
PDB; 2V8W; X-ray; 2.30 A; A/E=1-217.
PDB; 2V8X; X-ray; 2.30 A; A/E=1-217.
PDB; 2V8Y; X-ray; 2.10 A; A/E=1-217.
PDB; 2W97; X-ray; 2.29 A; A/B=1-217.
PDB; 3AM7; X-ray; 2.20 A; A=27-217.
PDB; 3TF2; X-ray; 2.10 A; A/B/C/D=1-217.
PDB; 3U7X; X-ray; 2.10 A; A/B=1-217.
PDB; 4AZA; X-ray; 2.16 A; A/C=1-217.
PDB; 4BEA; X-ray; 2.57 A; A=1-217.
PDB; 4DT6; X-ray; 2.60 A; A=1-217.
PDB; 4DUM; X-ray; 2.95 A; A=1-217.
PDB; 4TPW; X-ray; 1.50 A; A/B=28-217.
PDB; 4TQB; X-ray; 1.59 A; A/B=28-217.
PDB; 4TQC; X-ray; 1.80 A; A/B=28-217.
PDB; 4UED; X-ray; 1.75 A; A=36-217.
PDB; 5EHC; X-ray; 2.40 A; A=1-217.
PDB; 5EI3; X-ray; 1.71 A; A=1-217.
PDB; 5EIR; X-ray; 2.69 A; A=1-217.
PDB; 5EKV; X-ray; 3.61 A; A/C=1-217.
PDB; 5GW6; X-ray; 1.97 A; A=23-217.
PDB; 5T46; X-ray; 1.53 A; A/C=1-217.
PDBsum; 1IPB; -.
PDBsum; 1IPC; -.
PDBsum; 1WKW; -.
PDBsum; 2GPQ; -.
PDBsum; 2V8W; -.
PDBsum; 2V8X; -.
PDBsum; 2V8Y; -.
PDBsum; 2W97; -.
PDBsum; 3AM7; -.
PDBsum; 3TF2; -.
PDBsum; 3U7X; -.
PDBsum; 4AZA; -.
PDBsum; 4BEA; -.
PDBsum; 4DT6; -.
PDBsum; 4DUM; -.
PDBsum; 4TPW; -.
PDBsum; 4TQB; -.
PDBsum; 4TQC; -.
PDBsum; 4UED; -.
PDBsum; 5EHC; -.
PDBsum; 5EI3; -.
PDBsum; 5EIR; -.
PDBsum; 5EKV; -.
PDBsum; 5GW6; -.
PDBsum; 5T46; -.
ProteinModelPortal; P06730; -.
SMR; P06730; -.
BioGrid; 108292; 50.
CORUM; P06730; -.
DIP; DIP-22N; -.
ELM; P06730; -.
IntAct; P06730; 45.
MINT; MINT-85626; -.
BindingDB; P06730; -.
ChEMBL; CHEMBL4848; -.
DrugBank; DB01649; 7-Methyl-Gpppa.
DrugBank; DB02716; 7-Methyl-Guanosine-5'-Triphosphate.
DrugBank; DB01960; 7n-Methyl-8-Hydroguanosine-5'-Diphosphate.
DrugBank; DB05165; LY2275796.
iPTMnet; P06730; -.
PhosphoSitePlus; P06730; -.
SwissPalm; P06730; -.
BioMuta; EIF4E; -.
DMDM; 1352435; -.
OGP; P06730; -.
REPRODUCTION-2DPAGE; IPI00027485; -.
EPD; P06730; -.
MaxQB; P06730; -.
PeptideAtlas; P06730; -.
PRIDE; P06730; -.
TopDownProteomics; P06730-1; -. [P06730-1]
DNASU; 1977; -.
Ensembl; ENST00000280892; ENSP00000280892; ENSG00000151247. [P06730-3]
Ensembl; ENST00000450253; ENSP00000389624; ENSG00000151247. [P06730-1]
Ensembl; ENST00000505992; ENSP00000425561; ENSG00000151247. [P06730-2]
GeneID; 1977; -.
KEGG; hsa:1977; -.
UCSC; uc003hue.3; human. [P06730-1]
CTD; 1977; -.
DisGeNET; 1977; -.
EuPathDB; HostDB:ENSG00000151247.12; -.
GeneCards; EIF4E; -.
H-InvDB; HIX0039231; -.
HGNC; HGNC:3287; EIF4E.
HPA; CAB004077; -.
HPA; CAB016316; -.
HPA; HPA051311; -.
MalaCards; EIF4E; -.
MIM; 133440; gene.
MIM; 615091; phenotype.
neXtProt; NX_P06730; -.
OpenTargets; ENSG00000151247; -.
Orphanet; 106; Autism.
PharmGKB; PA27714; -.
GeneTree; ENSGT00520000055549; -.
HOGENOM; HOG000186751; -.
HOVERGEN; HBG006130; -.
InParanoid; P06730; -.
KO; K03259; -.
OMA; HLFKHPL; -.
OrthoDB; EOG091G0IVA; -.
PhylomeDB; P06730; -.
TreeFam; TF101526; -.
Reactome; R-HSA-1169408; ISG15 antiviral mechanism.
Reactome; R-HSA-156827; L13a-mediated translational silencing of Ceruloplasmin expression.
Reactome; R-HSA-159227; Transport of the SLBP independent Mature mRNA.
Reactome; R-HSA-159230; Transport of the SLBP Dependant Mature mRNA.
Reactome; R-HSA-159231; Transport of Mature mRNA Derived from an Intronless Transcript.
Reactome; R-HSA-166208; mTORC1-mediated signalling.
Reactome; R-HSA-429947; Deadenylation of mRNA.
Reactome; R-HSA-72649; Translation initiation complex formation.
Reactome; R-HSA-72662; Activation of the mRNA upon binding of the cap-binding complex and eIFs, and subsequent binding to 43S.
Reactome; R-HSA-72702; Ribosomal scanning and start codon recognition.
Reactome; R-HSA-72706; GTP hydrolysis and joining of the 60S ribosomal subunit.
SignaLink; P06730; -.
SIGNOR; P06730; -.
ChiTaRS; EIF4E; human.
EvolutionaryTrace; P06730; -.
GeneWiki; EIF4E; -.
GenomeRNAi; 1977; -.
PRO; PR:P06730; -.
Proteomes; UP000005640; Chromosome 4.
Bgee; ENSG00000151247; -.
CleanEx; HS_EIF4E; -.
ExpressionAtlas; P06730; baseline and differential.
Genevisible; P06730; HS.
GO; GO:0033391; C:chromatoid body; IEA:Ensembl.
GO; GO:0005737; C:cytoplasm; IDA:AgBase.
GO; GO:0036464; C:cytoplasmic ribonucleoprotein granule; IDA:HPA.
GO; GO:0010494; C:cytoplasmic stress granule; IDA:UniProtKB.
GO; GO:0005829; C:cytosol; IDA:UniProtKB.
GO; GO:0016281; C:eukaryotic translation initiation factor 4F complex; IDA:UniProtKB.
GO; GO:0070062; C:extracellular exosome; IDA:UniProtKB.
GO; GO:0005845; C:mRNA cap binding complex; IDA:UniProtKB.
GO; GO:0000932; C:P-body; IDA:MGI.
GO; GO:0048471; C:perinuclear region of cytoplasm; IDA:AgBase.
GO; GO:0016442; C:RISC complex; IDA:MGI.
GO; GO:0019899; F:enzyme binding; IDA:AgBase.
GO; GO:0031370; F:eukaryotic initiation factor 4G binding; IDA:AgBase.
GO; GO:0070491; F:repressing transcription factor binding; IDA:AgBase.
GO; GO:0000340; F:RNA 7-methylguanosine cap binding; IDA:UniProtKB.
GO; GO:0003723; F:RNA binding; IDA:UniProtKB.
GO; GO:0000339; F:RNA cap binding; TAS:ProtInc.
GO; GO:0003743; F:translation initiation factor activity; IDA:UniProtKB.
GO; GO:0001662; P:behavioral fear response; IEA:Ensembl.
GO; GO:0071549; P:cellular response to dexamethasone stimulus; IEA:Ensembl.
GO; GO:0000082; P:G1/S transition of mitotic cell cycle; IMP:UniProtKB.
GO; GO:0030324; P:lung development; IEA:Ensembl.
GO; GO:0006406; P:mRNA export from nucleus; TAS:Reactome.
GO; GO:0045665; P:negative regulation of neuron differentiation; IEA:Ensembl.
GO; GO:0017148; P:negative regulation of translation; IEA:Ensembl.
GO; GO:0000289; P:nuclear-transcribed mRNA poly(A) tail shortening; TAS:Reactome.
GO; GO:0045931; P:positive regulation of mitotic cell cycle; IMP:UniProtKB.
GO; GO:0006417; P:regulation of translation; IDA:UniProtKB.
GO; GO:0006405; P:RNA export from nucleus; TAS:Reactome.
GO; GO:0019827; P:stem cell population maintenance; IEA:Ensembl.
GO; GO:0006413; P:translational initiation; TAS:Reactome.
GO; GO:0016032; P:viral process; IEA:UniProtKB-KW.
Gene3D; 3.30.760.10; -; 1.
InterPro; IPR023398; TIF_eIF4e-like.
InterPro; IPR001040; TIF_eIF_4E.
InterPro; IPR019770; TIF_eIF_4E_CS.
PANTHER; PTHR11960; PTHR11960; 1.
Pfam; PF01652; IF4E; 1.
SUPFAM; SSF55418; SSF55418; 1.
PROSITE; PS00813; IF4E; 1.
1: Evidence at protein level;
3D-structure; Acetylation; Alternative splicing; Autism;
Autism spectrum disorder; Chromosomal rearrangement;
Complete proteome; Cytoplasm; Direct protein sequencing;
Host-virus interaction; Initiation factor; Phosphoprotein;
Protein biosynthesis; Reference proteome; RNA-binding;
Translation regulation.
INIT_MET 1 1 Removed. {ECO:0000244|PubMed:19413330,
ECO:0000269|PubMed:17036047}.
CHAIN 2 217 Eukaryotic translation initiation factor
4E.
/FTId=PRO_0000193634.
REGION 37 40 EIF4EBP1/2/3 binding.
REGION 56 57 7-methylguanosine-containing mRNA cap
binding.
REGION 73 77 EIF4EBP1/2/3 binding.
REGION 102 103 7-methylguanosine-containing mRNA cap
binding.
REGION 132 139 EIF4EBP1/2/3 binding.
REGION 157 162 7-methylguanosine-containing mRNA cap
binding.
REGION 205 207 7-methylguanosine-containing mRNA cap
binding.
MOD_RES 2 2 N-acetylalanine.
{ECO:0000244|PubMed:19413330}.
MOD_RES 22 22 Phosphothreonine.
{ECO:0000244|PubMed:23186163}.
MOD_RES 209 209 Phosphoserine; by PKC and MKNK2.
{ECO:0000269|PubMed:11154262,
ECO:0000269|PubMed:7665584,
ECO:0000269|PubMed:7782323}.
VAR_SEQ 1 6 MATVEP -> MLDLTSRGQVGTSRRMAEAACSAHFL (in
isoform 3).
{ECO:0000303|PubMed:14702039}.
/FTId=VSP_043591.
VAR_SEQ 133 133 T -> TRWDLAMLPRLVSNFWPQVILPLQPPKVLELQ (in
isoform 2).
{ECO:0000303|PubMed:16341674}.
/FTId=VSP_042014.
MUTAGEN 53 53 S->A,D: No effect on phosphorylation
level nor incorporation into eIF4F
complex. {ECO:0000269|PubMed:7590282,
ECO:0000269|PubMed:8505316}.
MUTAGEN 73 73 W->A: Abolishes binding to EIF4EBP1.
{ECO:0000269|PubMed:22578813}.
MUTAGEN 102 102 W->L: Decrease in mRNA cap binding; when
associated with A-105.
{ECO:0000269|PubMed:1672854}.
MUTAGEN 103 103 E->A: No effect.
{ECO:0000269|PubMed:1672854}.
MUTAGEN 104 104 D->A: No effect.
{ECO:0000269|PubMed:1672854}.
MUTAGEN 105 105 E->A: Decrease in mRNA cap binding; when
associated with L-102.
{ECO:0000269|PubMed:1672854}.
MUTAGEN 119 119 K->A: Higher affinity for EIF4G1.
{ECO:0000269|PubMed:17036047}.
CONFLICT 127 127 D -> N (in Ref. 5; AAH12611).
{ECO:0000305}.
HELIX 31 33 {ECO:0000244|PDB:5EI3}.
STRAND 38 49 {ECO:0000244|PDB:4TPW}.
STRAND 51 53 {ECO:0000244|PDB:5GW6}.
HELIX 56 59 {ECO:0000244|PDB:4TPW}.
STRAND 60 68 {ECO:0000244|PDB:4TPW}.
HELIX 69 82 {ECO:0000244|PDB:4TPW}.
STRAND 89 95 {ECO:0000244|PDB:4TPW}.
STRAND 100 103 {ECO:0000244|PDB:2GPQ}.
TURN 105 109 {ECO:0000244|PDB:4TPW}.
STRAND 111 116 {ECO:0000244|PDB:4TPW}.
HELIX 119 122 {ECO:0000244|PDB:4TPW}.
TURN 123 125 {ECO:0000244|PDB:4TPW}.
HELIX 126 138 {ECO:0000244|PDB:4TPW}.
TURN 139 142 {ECO:0000244|PDB:4TPW}.
HELIX 143 148 {ECO:0000244|PDB:4TPW}.
STRAND 149 155 {ECO:0000244|PDB:4TPW}.
STRAND 162 168 {ECO:0000244|PDB:4TPW}.
HELIX 173 187 {ECO:0000244|PDB:4TPW}.
STRAND 191 193 {ECO:0000244|PDB:4TQC}.
STRAND 196 199 {ECO:0000244|PDB:4TPW}.
HELIX 200 204 {ECO:0000244|PDB:4TPW}.
STRAND 205 207 {ECO:0000244|PDB:3AM7}.
TURN 208 210 {ECO:0000244|PDB:4TPW}.
STRAND 214 216 {ECO:0000244|PDB:4TPW}.
SEQUENCE 217 AA; 25097 MW; B869B8DE615E699D CRC64;
MATVEPETTP TPNPPTTEEE KTESNQEVAN PEHYIKHPLQ NRWALWFFKN DKSKTWQANL
RLISKFDTVE DFWALYNHIQ LSSNLMPGCD YSLFKDGIEP MWEDEKNKRG GRWLITLNKQ
QRRSDLDRFW LETLLCLIGE SFDDYSDDVC GAVVNVRAKG DKIAIWTTEC ENREAVTHIG
RVYKERLGLP PKIVIGYQSH ADTATKSGST TKNRFVV


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