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Database: UniProt
Entry: Q04637
LinkDB: Q04637
Original site: Q04637 
ID   IF4G1_HUMAN             Reviewed;        1599 AA.
AC   Q04637; D3DNT2; D3DNT4; D3DNT5; E9PFM1; G5E9S1; O43177; O95066; Q5HYG0;
AC   Q6ZN21; Q8N102;
DT   01-FEB-1995, integrated into UniProtKB/Swiss-Prot.
DT   20-APR-2010, sequence version 4.
DT   27-MAR-2024, entry version 243.
DE   RecName: Full=Eukaryotic translation initiation factor 4 gamma 1;
DE            Short=eIF-4-gamma 1;
DE            Short=eIF-4G 1;
DE            Short=eIF-4G1;
DE   AltName: Full=p220;
GN   Name=EIF4G1; Synonyms=EIF4F, EIF4G, EIF4GI;
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] (ISOFORM 7), AND VARIANT VAL-432.
RC   TISSUE=Brain;
RX   PubMed=1429670; DOI=10.1016/s0021-9258(18)50080-6;
RA   Yan R., Rychlik W., Etchison D., Rhoads R.E.;
RT   "Amino acid sequence of the human protein synthesis initiation factor eIF-4
RT   gamma.";
RL   J. Biol. Chem. 267:23226-23231(1992).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM B), AND INTERACTION WITH PABPC1.
RX   PubMed=9857202; DOI=10.1093/emboj/17.24.7480;
RA   Imataka H., Gradi A., Sonenberg N.;
RT   "A newly identified N-terminal amino acid sequence of human eIF4G binds
RT   poly(A)-binding protein and functions in poly(A)-dependent translation.";
RL   EMBO J. 17:7480-7489(1998).
RN   [3]
RP   NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM C).
RX   PubMed=9418880; DOI=10.1128/mcb.18.1.334;
RA   Gradi A., Imataka H., Svitkin Y.V., Rom E., Raught B., Morino S.,
RA   Sonenberg N.;
RT   "A novel functional human eukaryotic translation initiation factor 4G.";
RL   Mol. Cell. Biol. 18:334-342(1998).
RN   [4]
RP   NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 8), VARIANTS ALA-161 AND VAL-432, AND
RP   ALTERNATIVE INITIATION.
RX   PubMed=12052860; DOI=10.1128/mcb.22.13.4499-4511.2002;
RA   Byrd M.P., Zamora M., Lloyd R.E.;
RT   "Generation of multiple isoforms of eukaryotic translation initiation
RT   factor 4GI by use of alternate translation initiation codons.";
RL   Mol. Cell. Biol. 22:4499-4511(2002).
RN   [5]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM A).
RX   PubMed=14702039; DOI=10.1038/ng1285;
RA   Ota T., Suzuki Y., Nishikawa T., Otsuki T., Sugiyama T., Irie R.,
RA   Wakamatsu A., Hayashi K., Sato H., Nagai K., Kimura K., Makita H.,
RA   Sekine M., Obayashi M., Nishi T., Shibahara T., Tanaka T., Ishii S.,
RA   Yamamoto J., Saito K., Kawai Y., Isono Y., Nakamura Y., Nagahari K.,
RA   Murakami K., Yasuda T., Iwayanagi T., Wagatsuma M., Shiratori A., Sudo H.,
RA   Hosoiri T., Kaku Y., Kodaira H., Kondo H., Sugawara M., Takahashi M.,
RA   Kanda K., Yokoi T., Furuya T., Kikkawa E., Omura Y., Abe K., Kamihara K.,
RA   Katsuta N., Sato K., Tanikawa M., Yamazaki M., Ninomiya K., Ishibashi T.,
RA   Yamashita H., Murakawa K., Fujimori K., Tanai H., Kimata M., Watanabe M.,
RA   Hiraoka S., Chiba Y., Ishida S., Ono Y., Takiguchi S., Watanabe S.,
RA   Yosida M., Hotuta T., Kusano J., Kanehori K., Takahashi-Fujii A., Hara H.,
RA   Tanase T.-O., Nomura Y., Togiya S., Komai F., Hara R., Takeuchi K.,
RA   Arita M., Imose N., Musashino K., Yuuki H., Oshima A., Sasaki N.,
RA   Aotsuka S., Yoshikawa Y., Matsunawa H., Ichihara T., Shiohata N., Sano S.,
RA   Moriya S., Momiyama H., Satoh N., Takami S., Terashima Y., Suzuki O.,
RA   Nakagawa S., Senoh A., Mizoguchi H., Goto Y., Shimizu F., Wakebe H.,
RA   Hishigaki H., Watanabe T., Sugiyama A., Takemoto M., Kawakami B.,
RA   Yamazaki M., Watanabe K., Kumagai A., Itakura S., Fukuzumi Y., Fujimori Y.,
RA   Komiyama M., Tashiro H., Tanigami A., Fujiwara T., Ono T., Yamada K.,
RA   Fujii Y., Ozaki K., Hirao M., Ohmori Y., Kawabata A., Hikiji T.,
RA   Kobatake N., Inagaki H., Ikema Y., Okamoto S., Okitani R., Kawakami T.,
RA   Noguchi S., Itoh T., Shigeta K., Senba T., Matsumura K., Nakajima Y.,
RA   Mizuno T., Morinaga M., Sasaki M., Togashi T., Oyama M., Hata H.,
RA   Watanabe M., Komatsu T., Mizushima-Sugano J., Satoh T., Shirai Y.,
RA   Takahashi Y., Nakagawa K., Okumura K., Nagase T., Nomura N., Kikuchi H.,
RA   Masuho Y., Yamashita R., Nakai K., Yada T., Nakamura Y., Ohara O.,
RA   Isogai T., Sugano S.;
RT   "Complete sequencing and characterization of 21,243 full-length human
RT   cDNAs.";
RL   Nat. Genet. 36:40-45(2004).
RN   [6]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM A), AND VARIANT ALA-161.
RC   TISSUE=Endometrial tumor;
RX   PubMed=17974005; DOI=10.1186/1471-2164-8-399;
RA   Bechtel S., Rosenfelder H., Duda A., Schmidt C.P., Ernst U.,
RA   Wellenreuther R., Mehrle A., Schuster C., Bahr A., Bloecker H., Heubner D.,
RA   Hoerlein A., Michel G., Wedler H., Koehrer K., Ottenwaelder B., Poustka A.,
RA   Wiemann S., Schupp I.;
RT   "The full-ORF clone resource of the German cDNA consortium.";
RL   BMC Genomics 8:399-399(2007).
RN   [7]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX   PubMed=16641997; DOI=10.1038/nature04728;
RA   Muzny D.M., Scherer S.E., Kaul R., Wang J., Yu J., Sudbrak R., Buhay C.J.,
RA   Chen R., Cree A., Ding Y., Dugan-Rocha S., Gill R., Gunaratne P.,
RA   Harris R.A., Hawes A.C., Hernandez J., Hodgson A.V., Hume J., Jackson A.,
RA   Khan Z.M., Kovar-Smith C., Lewis L.R., Lozado R.J., Metzker M.L.,
RA   Milosavljevic A., Miner G.R., Morgan M.B., Nazareth L.V., Scott G.,
RA   Sodergren E., Song X.-Z., Steffen D., Wei S., Wheeler D.A., Wright M.W.,
RA   Worley K.C., Yuan Y., Zhang Z., Adams C.Q., Ansari-Lari M.A., Ayele M.,
RA   Brown M.J., Chen G., Chen Z., Clendenning J., Clerc-Blankenburg K.P.,
RA   Chen R., Chen Z., Davis C., Delgado O., Dinh H.H., Dong W., Draper H.,
RA   Ernst S., Fu G., Gonzalez-Garay M.L., Garcia D.K., Gillett W., Gu J.,
RA   Hao B., Haugen E., Havlak P., He X., Hennig S., Hu S., Huang W.,
RA   Jackson L.R., Jacob L.S., Kelly S.H., Kube M., Levy R., Li Z., Liu B.,
RA   Liu J., Liu W., Lu J., Maheshwari M., Nguyen B.-V., Okwuonu G.O.,
RA   Palmeiri A., Pasternak S., Perez L.M., Phelps K.A., Plopper F.J., Qiang B.,
RA   Raymond C., Rodriguez R., Saenphimmachak C., Santibanez J., Shen H.,
RA   Shen Y., Subramanian S., Tabor P.E., Verduzco D., Waldron L., Wang J.,
RA   Wang J., Wang Q., Williams G.A., Wong G.K.-S., Yao Z., Zhang J., Zhang X.,
RA   Zhao G., Zhou J., Zhou Y., Nelson D., Lehrach H., Reinhardt R.,
RA   Naylor S.L., Yang H., Olson M., Weinstock G., Gibbs R.A.;
RT   "The DNA sequence, annotation and analysis of human chromosome 3.";
RL   Nature 440:1194-1198(2006).
RN   [8]
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 (SEP-2005) to the EMBL/GenBank/DDBJ databases.
RN   [9]
RP   NUCLEOTIDE SEQUENCE [MRNA] OF 30-206, NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF
RP   180-234, VARIANT ALA-161, AND INTERACTION WITH ROTAVIRAL NSP3.
RX   PubMed=9755181; DOI=10.1093/emboj/17.19.5811;
RA   Piron M., Vende P., Cohen J., Poncet D.;
RT   "Rotavirus RNA binding protein NSP3, interacts with eIF-4GI and evicts the
RT   poly(A) binding protein from eIF4F.";
RL   EMBO J. 17:5811-5821(1998).
RN   [10]
RP   NUCLEOTIDE SEQUENCE [MRNA] OF 37-1599 (ISOFORM 8), INTERACTION WITH EIF4A,
RP   VARIANTS ALA-161 AND VAL-432, AND MUTAGENESIS OF LEU-768; LEU-771; PHE-776;
RP   842-LEU-LEU-843; 851-PHE-GLU-852; LEU-896; ILE-902; LEU-905; ARG-974;
RP   PHE-977; LEU-985 AND TRP-990.
RX   PubMed=9372926; DOI=10.1128/mcb.17.12.6940;
RA   Imataka H., Sonenberg N.;
RT   "Human eukaryotic translation initiation factor 4G (eIF4G) possesses two
RT   separate and independent binding sites for eIF4A.";
RL   Mol. Cell. Biol. 17:6940-6947(1997).
RN   [11]
RP   NUCLEOTIDE SEQUENCE [MRNA] OF 605-721, INTERACTION WITH EIF4E, AND
RP   MUTAGENESIS OF TYR-612 AND 617-LEU-LEU-618.
RX   PubMed=7651417; DOI=10.1128/mcb.15.9.4990;
RA   Mader S., Lee H., Pause A., Sonenberg N.;
RT   "The translation initiation factor eIF-4E binds to a common motif shared by
RT   the translation factor eIF-4 gamma and the translational repressors 4E-
RT   binding proteins.";
RL   Mol. Cell. Biol. 15:4990-4997(1995).
RN   [12]
RP   NUCLEOTIDE SEQUENCE [MRNA] OF 682-912 (ISOFORM 8).
RA   De Gregorio E.;
RL   Submitted (AUG-1997) to the EMBL/GenBank/DDBJ databases.
RN   [13]
RP   CLEAVAGE BY RHINOVIRUS AND COXSACKIEVIRUS PROTEASE.
RX   PubMed=8396129; DOI=10.1016/s0021-9258(19)36499-3;
RA   Lamphear B.J., Yan R., Yang F., Waters D., Liebig H.-D., Klump H.,
RA   Kuechler E., Skern T., Rhoads R.E.;
RT   "Mapping the cleavage site in protein synthesis initiation factor eIF-4
RT   gamma of the 2A proteases from human Coxsackievirus and rhinovirus.";
RL   J. Biol. Chem. 268:19200-19203(1993).
RN   [14]
RP   INTERACTION WITH EIF4E.
RC   TISSUE=Placenta;
RX   PubMed=7935836; DOI=10.1038/371762a0;
RA   Pause A., Belsham G.J., Gingras A.-C., Donze O., Lin T.-A.,
RA   Lawrence J.C. Jr., Sonenberg N.;
RT   "Insulin-dependent stimulation of protein synthesis by phosphorylation of a
RT   regulator of 5'-cap function.";
RL   Nature 371:762-767(1994).
RN   [15]
RP   INTERACTION WITH EIF4E AND EIF4EBP1.
RX   PubMed=8521827; DOI=10.1002/j.1460-2075.1995.tb00257.x;
RA   Haghighat A., Mader S., Pause A., Sonenberg N.;
RT   "Repression of cap-dependent translation by 4E-binding protein 1:
RT   competition with p220 for binding to eukaryotic initiation factor-4E.";
RL   EMBO J. 14:5701-5709(1995).
RN   [16]
RP   MUTAGENESIS OF GLY-682.
RX   PubMed=8961935; DOI=10.1021/bi961864t;
RA   Lamphear B.J., Rhoads R.E.;
RT   "A single amino acid change in protein synthesis initiation factor 4G
RT   renders cap-dependent translation resistant to picornaviral 2A proteases.";
RL   Biochemistry 35:15726-15733(1996).
RN   [17]
RP   CLEAVAGE BY POLIOVIRUS.
RX   PubMed=9755863; DOI=10.1016/s0014-5793(98)01027-8;
RA   Ventoso I., MacMillan S.E., Hershey J.W., Carrasco L.;
RT   "Poliovirus 2A proteinase cleaves directly the eIF-4G subunit of eIF-4F
RT   complex.";
RL   FEBS Lett. 435:79-83(1998).
RN   [18]
RP   REVIEW.
RX   PubMed=10872469; DOI=10.1146/annurev.biochem.68.1.913;
RA   Gingras A.-C., Raught B., Sonenberg N.;
RT   "eIF4 initiation factors: effectors of mRNA recruitment to ribosomes and
RT   regulators of translation.";
RL   Annu. Rev. Biochem. 68:913-963(1999).
RN   [19]
RP   INTERACTION WITH MKNK1.
RX   PubMed=9878069; DOI=10.1093/emboj/18.1.270;
RA   Pyronnet S., Imataka H., Gingras A.-C., Fukunaga R., Hunter T.,
RA   Sonenberg N.;
RT   "Human eukaryotic translation initiation factor 4G (eIF4G) recruits mnk1 to
RT   phosphorylate eIF4E.";
RL   EMBO J. 18:270-279(1999).
RN   [20]
RP   INTERACTION WITH PABPC1, AND MUTAGENESIS OF 174-LYS--LYS-178 AND
RP   184-ASP--GLN-197.
RX   PubMed=10996799; DOI=10.1016/s0960-9822(00)00701-6;
RA   Wakiyama M., Imataka H., Sonenberg N.;
RT   "Interaction of eIF4G with poly(A)-binding protein stimulates translation
RT   and is critical for Xenopus oocyte maturation.";
RL   Curr. Biol. 10:1147-1150(2000).
RN   [21]
RP   INTERACTION WITH PABPC1.
RX   PubMed=10970864; DOI=10.1093/emboj/19.17.4723;
RA   Gray N.K., Coller J.M., Dickson K.S., Wickens M.;
RT   "Multiple portions of poly(A)-binding protein stimulate translation in
RT   vivo.";
RL   EMBO J. 19:4723-4733(2000).
RN   [22]
RP   CLEAVAGE BY FMDV AND HRV-2.
RX   PubMed=11034318; DOI=10.1016/s0014-5793(00)01928-1;
RA   Glaser W., Skern T.;
RT   "Extremely efficient cleavage of eIF4G by picornaviral proteinases L and 2A
RT   in vitro.";
RL   FEBS Lett. 480:151-155(2000).
RN   [23]
RP   INTERACTION WITH MKNK2.
RX   PubMed=11154262; DOI=10.1128/mcb.21.3.743-754.2001;
RA   Scheper G.C., Morrice N.A., Kleijn M., Proud C.G.;
RT   "The mitogen-activated protein kinase signal-integrating kinase Mnk2 is a
RT   eukaryotic initiation factor 4E kinase with high levels of basal activity
RT   in mammalian cells.";
RL   Mol. Cell. Biol. 21:743-754(2001).
RN   [24]
RP   INTERACTION WITH HADV5 100K PROTEIN (MICROBIAL INFECTION).
RX   PubMed=15314025; DOI=10.1101/gad.1212504;
RA   Xi Q., Cuesta R., Schneider R.J.;
RT   "Tethering of eIF4G to adenoviral mRNAs by viral 100k protein drives
RT   ribosome shunting.";
RL   Genes Dev. 18:1997-2009(2004).
RN   [25]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-1231, AND IDENTIFICATION BY
RP   MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC   TISSUE=Cervix carcinoma;
RX   PubMed=17081983; DOI=10.1016/j.cell.2006.09.026;
RA   Olsen J.V., Blagoev B., Gnad F., Macek B., Kumar C., Mortensen P., Mann M.;
RT   "Global, in vivo, and site-specific phosphorylation dynamics in signaling
RT   networks.";
RL   Cell 127:635-648(2006).
RN   [26]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-1231, AND IDENTIFICATION BY
RP   MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC   TISSUE=Cervix carcinoma;
RX   PubMed=16964243; DOI=10.1038/nbt1240;
RA   Beausoleil S.A., Villen J., Gerber S.A., Rush J., Gygi S.P.;
RT   "A probability-based approach for high-throughput protein phosphorylation
RT   analysis and site localization.";
RL   Nat. Biotechnol. 24:1285-1292(2006).
RN   [27]
RP   INTERACTION WITH CIRBP.
RX   PubMed=16513844; DOI=10.1093/nar/gkj519;
RA   Yang R., Weber D.J., Carrier F.;
RT   "Post-transcriptional regulation of thioredoxin by the stress inducible
RT   heterogeneous ribonucleoprotein A18.";
RL   Nucleic Acids Res. 34:1224-1236(2006).
RN   [28]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-1092, AND IDENTIFICATION BY
RP   MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC   TISSUE=Cervix carcinoma;
RX   PubMed=17924679; DOI=10.1021/pr070152u;
RA   Yu L.R., Zhu Z., Chan K.C., Issaq H.J., Dimitrov D.S., Veenstra T.D.;
RT   "Improved titanium dioxide enrichment of phosphopeptides from HeLa cells
RT   and high confident phosphopeptide identification by cross-validation of
RT   MS/MS and MS/MS/MS spectra.";
RL   J. Proteome Res. 6:4150-4162(2007).
RN   [29]
RP   INTERACTION WITH RBM4.
RX   PubMed=17284590; DOI=10.1073/pnas.0611015104;
RA   Lin J.C., Hsu M., Tarn W.Y.;
RT   "Cell stress modulates the function of splicing regulatory protein RBM4 in
RT   translation control.";
RL   Proc. Natl. Acad. Sci. U.S.A. 104:2235-2240(2007).
RN   [30]
RP   IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC   TISSUE=Platelet;
RX   PubMed=18088087; DOI=10.1021/pr0704130;
RA   Zahedi R.P., Lewandrowski U., Wiesner J., Wortelkamp S., Moebius J.,
RA   Schuetz C., Walter U., Gambaryan S., Sickmann A.;
RT   "Phosphoproteome of resting human platelets.";
RL   J. Proteome Res. 7:526-534(2008).
RN   [31]
RP   INTERACTION WITH ROTAVIRUS A NSP3 (MICROBIAL INFECTION).
RX   PubMed=18799579; DOI=10.1128/jvi.00872-08;
RA   Harb M., Becker M.M., Vitour D., Baron C.H., Vende P., Brown S.C.,
RA   Bolte S., Arold S.T., Poncet D.;
RT   "Nuclear localization of cytoplasmic poly(A)-binding protein upon rotavirus
RT   infection involves the interaction of NSP3 with eIF4G and RoXaN.";
RL   J. Virol. 82:11283-11293(2008).
RN   [32]
RP   INTERACTION WITH DAZAP2, AND SUBCELLULAR LOCATION.
RX   PubMed=17984221; DOI=10.1128/mcb.01226-07;
RA   Kim J.E., Ryu I., Kim W.J., Song O.K., Ryu J., Kwon M.Y., Kim J.H.,
RA   Jang S.K.;
RT   "Proline-rich transcript in brain protein induces stress granule
RT   formation.";
RL   Mol. Cell. Biol. 28:803-813(2008).
RN   [33]
RP   INTERACTION WITH MIF4GD.
RX   PubMed=18025107; DOI=10.1128/mcb.01500-07;
RA   Cakmakci N.G., Lerner R.S., Wagner E.J., Zheng L., Marzluff W.F.;
RT   "SLIP1, a factor required for activation of histone mRNA translation by the
RT   stem-loop binding protein.";
RL   Mol. Cell. Biol. 28:1182-1194(2008).
RN   [34]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-207; THR-223; THR-647;
RP   SER-1092 AND SER-1209, AND IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE
RP   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   [35]
RP   IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX   PubMed=19369195; DOI=10.1074/mcp.m800588-mcp200;
RA   Oppermann F.S., Gnad F., Olsen J.V., Hornberger R., Greff Z., Keri G.,
RA   Mann M., Daub H.;
RT   "Large-scale proteomics analysis of the human kinome.";
RL   Mol. Cell. Proteomics 8:1751-1764(2009).
RN   [36]
RP   IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC   TISSUE=Leukemic T-cell;
RX   PubMed=19690332; DOI=10.1126/scisignal.2000007;
RA   Mayya V., Lundgren D.H., Hwang S.-I., Rezaul K., Wu L., Eng J.K.,
RA   Rodionov V., Han D.K.;
RT   "Quantitative phosphoproteomic analysis of T cell receptor signaling
RT   reveals system-wide modulation of protein-protein interactions.";
RL   Sci. Signal. 2:RA46-RA46(2009).
RN   [37]
RP   ACETYLATION [LARGE SCALE ANALYSIS] AT LYS-1095, AND IDENTIFICATION BY MASS
RP   SPECTROMETRY [LARGE SCALE ANALYSIS].
RX   PubMed=19608861; DOI=10.1126/science.1175371;
RA   Choudhary C., Kumar C., Gnad F., Nielsen M.L., Rehman M., Walther T.C.,
RA   Olsen J.V., Mann M.;
RT   "Lysine acetylation targets protein complexes and co-regulates major
RT   cellular functions.";
RL   Science 325:834-840(2009).
RN   [38]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-1028; SER-1092; SER-1185;
RP   SER-1187; SER-1209; THR-1211; SER-1231 AND SER-1596, 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   [39]
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   [40]
RP   PHOSPHORYLATION AT SER-1185.
RX   PubMed=21576361; DOI=10.1128/mcb.05589-11;
RA   Dobrikov M., Dobrikova E., Shveygert M., Gromeier M.;
RT   "Phosphorylation of eukaryotic translation initiation factor 4G1 (eIF4G1)
RT   by protein kinase C{alpha} regulates eIF4G1 binding to Mnk1.";
RL   Mol. Cell. Biol. 31:2947-2959(2011).
RN   [41]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-1028; SER-1092; SER-1145;
RP   SER-1147; SER-1185; SER-1187; SER-1209; THR-1211; SER-1231 AND SER-1596,
RP   AND IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX   PubMed=21406692; DOI=10.1126/scisignal.2001570;
RA   Rigbolt K.T., Prokhorova T.A., Akimov V., Henningsen J., Johansen P.T.,
RA   Kratchmarova I., Kassem M., Mann M., Olsen J.V., Blagoev B.;
RT   "System-wide temporal characterization of the proteome and phosphoproteome
RT   of human embryonic stem cell differentiation.";
RL   Sci. Signal. 4:RS3-RS3(2011).
RN   [42]
RP   INTERACTION WITH DDX3X, AND SUBCELLULAR LOCATION.
RX   PubMed=22872150; DOI=10.1038/emboj.2012.220;
RA   Soto-Rifo R., Rubilar P.S., Limousin T., de Breyne S., Decimo D.,
RA   Ohlmann T.;
RT   "DEAD-box protein DDX3 associates with eIF4F to promote translation of
RT   selected mRNAs.";
RL   EMBO J. 31:3745-3756(2012).
RN   [43]
RP   ACETYLATION [LARGE SCALE ANALYSIS] AT MET-2 (ISOFORM C), CLEAVAGE OF
RP   INITIATOR METHIONINE [LARGE SCALE ANALYSIS] (ISOFORM C), AND IDENTIFICATION
RP   BY MASS SPECTROMETRY [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   [44]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-207; THR-647; SER-1028;
RP   SER-1077; SER-1092; SER-1145; SER-1147; SER-1185; SER-1187; SER-1194;
RP   SER-1209; SER-1231; SER-1238 AND SER-1596, PHOSPHORYLATION [LARGE SCALE
RP   ANALYSIS] AT SER-509 (ISOFORM 7), PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT
RP   SER-705 (ISOFORM 8), AND IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE
RP   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   [45]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-314, 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   [46]
RP   METHYLATION [LARGE SCALE ANALYSIS] AT ARG-73; ARG-110; ARG-685; ARG-694;
RP   ARG-1032 AND ARG-1042, METHYLATION [LARGE SCALE ANALYSIS] AT ARG-489 AND
RP   ARG-498 (ISOFORM 7), METHYLATION [LARGE SCALE ANALYSIS] AT ARG-685 AND
RP   ARG-694 (ISOFORM 8), AND IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE
RP   ANALYSIS].
RC   TISSUE=Colon carcinoma;
RX   PubMed=24129315; DOI=10.1074/mcp.o113.027870;
RA   Guo A., Gu H., Zhou J., Mulhern D., Wang Y., Lee K.A., Yang V., Aguiar M.,
RA   Kornhauser J., Jia X., Ren J., Beausoleil S.A., Silva J.C., Vemulapalli V.,
RA   Bedford M.T., Comb M.J.;
RT   "Immunoaffinity enrichment and mass spectrometry analysis of protein
RT   methylation.";
RL   Mol. Cell. Proteomics 13:372-387(2014).
RN   [47]
RP   INTERACTION WITH HNRNPD, AND RNA-BINDING.
RX   PubMed=24423872; DOI=10.1093/nar/gkt1379;
RA   Lee K.H., Kim S.H., Kim H.J., Kim W., Lee H.R., Jung Y., Choi J.H.,
RA   Hong K.Y., Jang S.K., Kim K.T.;
RT   "AUF1 contributes to Cryptochrome1 mRNA degradation and rhythmic
RT   translation.";
RL   Nucleic Acids Res. 42:3590-3606(2014).
RN   [48]
RP   FUNCTION.
RX   PubMed=29062139; DOI=10.1038/s41598-017-14262-7;
RA   Adjibade P., Grenier St-Sauveur V., Bergeman J., Huot M.E., Khandjian E.W.,
RA   Mazroui R.;
RT   "DDX3 regulates endoplasmic reticulum stress-induced ATF4 expression.";
RL   Sci. Rep. 7:13832-13832(2017).
RN   [49]
RP   FUNCTION, AND INTERACTION WITH EIF1 AND EIF4E.
RX   PubMed=29987188; DOI=10.1128/mcb.00139-18;
RA   Haimov O., Sehrawat U., Tamarkin-Ben Harush A., Bahat A., Uzonyi A.,
RA   Will A., Hiraishi H., Asano K., Dikstein R.;
RT   "Dynamic interaction of eukaryotic initiation factor 4G1 (eIF4G1) with
RT   eIF4E and eIF1 underlies scanning-dependent and -independent translation.";
RL   Mol. Cell. Biol. 38:0-0(2018).
RN   [50]
RP   VARIANT [LARGE SCALE ANALYSIS] VAL-432, AND IDENTIFICATION BY MASS
RP   SPECTROMETRY [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   [51]
RP   VARIANT HIS-201.
RX   PubMed=26740508; DOI=10.1136/jmedgenet-2015-103568;
RA   Lopes F., Barbosa M., Ameur A., Soares G., de Sa J., Dias A.I.,
RA   Oliveira G., Cabral P., Temudo T., Calado E., Cruz I.F., Vieira J.P.,
RA   Oliveira R., Esteves S., Sauer S., Jonasson I., Syvaenen A.C.,
RA   Gyllensten U., Pinto D., Maciel P.;
RT   "Identification of novel genetic causes of Rett syndrome-like phenotypes.";
RL   J. Med. Genet. 53:190-199(2016).
RN   [52]
RP   X-RAY CRYSTALLOGRAPHY (2.38 ANGSTROMS) OF 172-199 IN COMPLEX WITH ROTAVIRAL
RP   NSP3, INTERACTION WITH PABPC1, AND MUTAGENESIS OF ILE-180; ILE-182; ILE-192
RP   AND ILE-196.
RX   PubMed=12086624; DOI=10.1016/s1097-2765(02)00555-5;
RA   Groft C.M., Burley S.K.;
RT   "Recognition of eIF4G by rotavirus NSP3 reveals a basis for mRNA
RT   circularization.";
RL   Mol. Cell 9:1273-1283(2002).
RN   [53]
RP   X-RAY CRYSTALLOGRAPHY (2.24 ANGSTROMS) OF 1234-1571.
RX   PubMed=16698552; DOI=10.1016/j.str.2006.03.012;
RA   Bellsolell L., Cho-Park P.F., Poulin F., Sonenberg N., Burley S.K.;
RT   "Two structurally atypical HEAT domains in the C-terminal portion of human
RT   eIF4G support binding to eIF4A and Mnk1.";
RL   Structure 14:913-923(2006).
RN   [54]
RP   VARIANT [LARGE SCALE ANALYSIS] LEU-696.
RX   PubMed=16959974; DOI=10.1126/science.1133427;
RA   Sjoeblom T., Jones S., Wood L.D., Parsons D.W., Lin J., Barber T.D.,
RA   Mandelker D., Leary R.J., Ptak J., Silliman N., Szabo S., Buckhaults P.,
RA   Farrell C., Meeh P., Markowitz S.D., Willis J., Dawson D., Willson J.K.V.,
RA   Gazdar A.F., Hartigan J., Wu L., Liu C., Parmigiani G., Park B.H.,
RA   Bachman K.E., Papadopoulos N., Vogelstein B., Kinzler K.W.,
RA   Velculescu V.E.;
RT   "The consensus coding sequences of human breast and colorectal cancers.";
RL   Science 314:268-274(2006).
RN   [55]
RP   VARIANTS PARK18 VAL-502 AND HIS-1205, AND VARIANTS SER-71; ALA-161;
RP   CYS-311; VAL-432; 466-GLY--ALA-468 DEL; CYS-686; VAL-806; SER-829;
RP   ARG-1164; TRP-1197; ALA-1229; PRO-1233 AND SER-1257.
RX   PubMed=21907011; DOI=10.1016/j.ajhg.2011.08.009;
RA   Chartier-Harlin M.C., Dachsel J.C., Vilarino-Guell C., Lincoln S.J.,
RA   Lepretre F., Hulihan M.M., Kachergus J., Milnerwood A.J., Tapia L.,
RA   Song M.S., Le Rhun E., Mutez E., Larvor L., Duflot A.,
RA   Vanbesien-Mailliot C., Kreisler A., Ross O.A., Nishioka K.,
RA   Soto-Ortolaza A.I., Cobb S.A., Melrose H.L., Behrouz B., Keeling B.H.,
RA   Bacon J.A., Hentati E., Williams L., Yanagiya A., Sonenberg N.,
RA   Lockhart P.J., Zubair A.C., Uitti R.J., Aasly J.O., Krygowska-Wajs A.,
RA   Opala G., Wszolek Z.K., Frigerio R., Maraganore D.M., Gosal D., Lynch T.,
RA   Hutchinson M., Bentivoglio A.R., Valente E.M., Nichols W.C., Pankratz N.,
RA   Foroud T., Gibson R.A., Hentati F., Dickson D.W., Destee A., Farrer M.J.;
RT   "Translation initiator EIF4G1 mutations in familial Parkinson disease.";
RL   Am. J. Hum. Genet. 89:398-406(2011).
CC   -!- FUNCTION: Component of the protein complex eIF4F, which is involved in
CC       the recognition of the mRNA cap, ATP-dependent unwinding of 5'-terminal
CC       secondary structure and recruitment of mRNA to the ribosome
CC       (PubMed:29987188). Exists in two complexes, either with EIF1 or with
CC       EIF4E (mutually exclusive) (PubMed:29987188). Together with EIF1, is
CC       required for leaky scanning, in particular for avoiding cap-proximal
CC       start codon (PubMed:29987188). Together with EIF4E, antagonizes the
CC       scanning promoted by EIF1-EIF4G1 and locates the start codon (through a
CC       TISU element) without scanning (PubMed:29987188). As a member of the
CC       eIF4F complex, required for endoplasmic reticulum stress-induced ATF4
CC       mRNA translation (PubMed:29062139). {ECO:0000269|PubMed:29062139,
CC       ECO:0000269|PubMed:29987188}.
CC   -!- SUBUNIT: eIF4F is a multi-subunit complex, the composition of which
CC       varies with external and internal environmental conditions. It is
CC       composed of at least EIF4A, EIF4E (cap-binding) and EIF4G1/EIF4G3
CC       (PubMed:9372926, PubMed:7651417, PubMed:7935836). Interacts with eIF3
CC       complex, mutually exclusive with EIF4A1 or EIF4A2, EIF4E and through
CC       its N-terminus with PABPC1 (PubMed:9857202, PubMed:9372926,
CC       PubMed:7651417, PubMed:7935836, PubMed:10996799, PubMed:10970864,
CC       PubMed:12086624, PubMed:16698552). Interacts with EIF4E or with EIF1
CC       (mutually exclusive) through a common binding site (PubMed:29987188).
CC       Interacts through its C-terminus with the serine/threonine kinases
CC       MKNK1, and with MKNK2 (PubMed:9878069, PubMed:11154262). Appears to act
CC       as a scaffold protein, holding these enzymes in place to phosphorylate
CC       EIF4E (PubMed:9878069, PubMed:11154262). Non-phosphorylated EIF4EBP1
CC       competes with EIF4G1/EIF4G3 to interact with EIF4E; insulin stimulated
CC       MAP-kinase (MAPK1 and MAPK3) phosphorylation of EIF4EBP1 causes
CC       dissociation of the complex allowing EIF4G1/EIF4G3 to bind and
CC       consequent initiation of translation (PubMed:8521827). EIF4G1/EIF4G3
CC       interacts with PABPC1 to bring about circularization of the mRNA
CC       (PubMed:9857202, PubMed:10996799, PubMed:10970864, PubMed:12086624).
CC       Interacts with EIF4E3 (By similarity). Interacts with CIRBP and MIF4GD
CC       (PubMed:10996799, PubMed:10970864, PubMed:16513844, PubMed:18025107).
CC       Interacts with RBM4 (PubMed:17284590). Interacts with HNRNPD/AUF1; the
CC       interaction requires RNA (PubMed:24423872). Interacts with DDX3X; the
CC       interaction requires RNA (PubMed:22872150). Interacts with DAZAP2
CC       (PubMed:17984221). {ECO:0000250|UniProtKB:Q6NZJ6,
CC       ECO:0000269|PubMed:10970864, ECO:0000269|PubMed:10996799,
CC       ECO:0000269|PubMed:11154262, ECO:0000269|PubMed:12086624,
CC       ECO:0000269|PubMed:16513844, ECO:0000269|PubMed:17284590,
CC       ECO:0000269|PubMed:17984221, ECO:0000269|PubMed:18025107,
CC       ECO:0000269|PubMed:22872150, ECO:0000269|PubMed:24423872,
CC       ECO:0000269|PubMed:29987188, ECO:0000269|PubMed:7651417,
CC       ECO:0000269|PubMed:7935836, ECO:0000269|PubMed:8521827,
CC       ECO:0000269|PubMed:9372926, ECO:0000269|PubMed:9857202,
CC       ECO:0000269|PubMed:9878069}.
CC   -!- SUBUNIT: (Microbial infection) Interacts with rotavirus A NSP3; in this
CC       interaction, NSP3 takes the place of PABPC1 thereby inducing shutoff of
CC       host protein synthesis. {ECO:0000269|PubMed:18799579,
CC       ECO:0000269|PubMed:9755181}.
CC   -!- SUBUNIT: (Microbial infection) Interacts with human adenovirus 5
CC       protein 100K; this interaction promotes translational shunt in presence
CC       of polysomes containing viral tripartite leader mRNAs.
CC       {ECO:0000269|PubMed:15314025}.
CC   -!- INTERACTION:
CC       Q04637; O00571: DDX3X; NbExp=3; IntAct=EBI-73711, EBI-353779;
CC       Q04637; O75822: EIF3J; NbExp=2; IntAct=EBI-73711, EBI-366647;
CC       Q04637; P60842: EIF4A1; NbExp=11; IntAct=EBI-73711, EBI-73449;
CC       Q04637; P06730: EIF4E; NbExp=10; IntAct=EBI-73711, EBI-73440;
CC       Q04637; Q04637: EIF4G1; NbExp=2; IntAct=EBI-73711, EBI-73711;
CC       Q04637; Q14103-4: HNRNPD; NbExp=3; IntAct=EBI-73711, EBI-432545;
CC       Q04637; P11940: PABPC1; NbExp=4; IntAct=EBI-73711, EBI-81531;
CC       Q04637; Q9BWF3-1: RBM4; NbExp=4; IntAct=EBI-73711, EBI-15621561;
CC       Q04637; Q9J0X9: UL54; Xeno; NbExp=3; IntAct=EBI-73711, EBI-7967856;
CC       Q04637-1; P60842: EIF4A1; NbExp=2; IntAct=EBI-5456295, EBI-73449;
CC       Q04637-9; Q9NQ94: A1CF; NbExp=3; IntAct=EBI-12012124, EBI-2809489;
CC       Q04637-9; Q8N5M1: ATPAF2; NbExp=3; IntAct=EBI-12012124, EBI-1166928;
CC       Q04637-9; Q2TAC2-2: CCDC57; NbExp=3; IntAct=EBI-12012124, EBI-10961624;
CC       Q04637-9; P55273: CDKN2D; NbExp=3; IntAct=EBI-12012124, EBI-745859;
CC       Q04637-9; Q99828: CIB1; NbExp=7; IntAct=EBI-12012124, EBI-372594;
CC       Q04637-9; P56545-3: CTBP2; NbExp=3; IntAct=EBI-12012124, EBI-10171902;
CC       Q04637-9; Q86UW9: DTX2; NbExp=3; IntAct=EBI-12012124, EBI-740376;
CC       Q04637-9; Q9H0I2: ENKD1; NbExp=3; IntAct=EBI-12012124, EBI-744099;
CC       Q04637-9; P51116: FXR2; NbExp=3; IntAct=EBI-12012124, EBI-740459;
CC       Q04637-9; Q15323: KRT31; NbExp=3; IntAct=EBI-12012124, EBI-948001;
CC       Q04637-9; O76011: KRT34; NbExp=3; IntAct=EBI-12012124, EBI-1047093;
CC       Q04637-9; Q96HA8: NTAQ1; NbExp=3; IntAct=EBI-12012124, EBI-741158;
CC       Q04637-9; Q9UBV8: PEF1; NbExp=3; IntAct=EBI-12012124, EBI-724639;
CC       Q04637-9; Q96GM5: SMARCD1; NbExp=3; IntAct=EBI-12012124, EBI-358489;
CC   -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000269|PubMed:17984221}. Nucleus
CC       {ECO:0000269|PubMed:17984221}. Cytoplasm, Stress granule
CC       {ECO:0000269|PubMed:22872150}.
CC   -!- ALTERNATIVE PRODUCTS:
CC       Event=Alternative splicing, Alternative initiation; Named isoforms=8;
CC       Name=A;
CC         IsoId=Q04637-1; Sequence=Displayed;
CC       Name=B;
CC         IsoId=Q04637-3; Sequence=VSP_018720;
CC       Name=C;
CC         IsoId=Q04637-4; Sequence=VSP_018721;
CC       Name=D;
CC         IsoId=Q04637-5; Sequence=VSP_018722;
CC       Name=E;
CC         IsoId=Q04637-6; Sequence=VSP_018723;
CC       Name=7;
CC         IsoId=Q04637-7; Sequence=VSP_018723, VSP_047397;
CC       Name=8;
CC         IsoId=Q04637-8; Sequence=VSP_047397;
CC       Name=9;
CC         IsoId=Q04637-9; Sequence=VSP_047396;
CC   -!- PTM: Phosphorylated at multiple sites in vivo. Phosphorylation at Ser-
CC       1185 by PRKCA induces binding to MKNK1. {ECO:0000269|PubMed:21576361}.
CC   -!- PTM: Following infection by certain enteroviruses, rhinoviruses and
CC       aphthoviruses, EIF4G1 is cleaved by the viral protease 2A, or the
CC       leader protease in the case of aphthoviruses. This shuts down the
CC       capped cellular mRNA transcription. {ECO:0000269|PubMed:11034318,
CC       ECO:0000269|PubMed:8396129, ECO:0000269|PubMed:9755863}.
CC   -!- DISEASE: Parkinson disease 18 (PARK18) [MIM:614251]: An autosomal
CC       dominant, late-onset form of Parkinson disease. Parkinson disease is a
CC       complex neurodegenerative disorder characterized by bradykinesia,
CC       resting tremor, muscular rigidity and postural instability, as well as
CC       by a clinically significant response to treatment with levodopa. The
CC       pathology involves the loss of dopaminergic neurons in the substantia
CC       nigra and the presence of Lewy bodies (intraneuronal accumulations of
CC       aggregated proteins), in surviving neurons in various areas of the
CC       brain. {ECO:0000269|PubMed:21907011}. Note=The disease is caused by
CC       variants affecting the gene represented in this entry.
CC   -!- MISCELLANEOUS: [Isoform B]: Produced by alternative initiation at Met-
CC       41 of isoform A. {ECO:0000305}.
CC   -!- MISCELLANEOUS: [Isoform C]: Produced by alternative initiation at Met-
CC       88 of isoform A. {ECO:0000305}.
CC   -!- MISCELLANEOUS: [Isoform D]: Produced by alternative initiation at Met-
CC       165 of isoform A. {ECO:0000305}.
CC   -!- MISCELLANEOUS: [Isoform E]: Produced by alternative initiation at Met-
CC       197 of isoform A. {ECO:0000305}.
CC   -!- MISCELLANEOUS: [Isoform 7]: Produced by alternative splicing.
CC       {ECO:0000305}.
CC   -!- MISCELLANEOUS: [Isoform 8]: Produced by alternative splicing.
CC       {ECO:0000305}.
CC   -!- MISCELLANEOUS: [Isoform 9]: Produced by alternative splicing.
CC       {ECO:0000305}.
CC   -!- SIMILARITY: Belongs to the eukaryotic initiation factor 4G family.
CC       {ECO:0000305}.
CC   -!- SEQUENCE CAUTION:
CC       Sequence=AAC78444.1; Type=Erroneous initiation; Note=Truncated N-terminus.; Evidence={ECO:0000305};
CC       Sequence=AAC82471.1; Type=Erroneous initiation; Note=Truncated N-terminus.; Evidence={ECO:0000305};
CC       Sequence=BAA02185.1; Type=Frameshift; Evidence={ECO:0000305};
CC       Sequence=BAD18554.1; Type=Miscellaneous discrepancy; Note=Aberrant splicing.; Evidence={ECO:0000305};
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DR   EMBL; D12686; BAA02185.1; ALT_FRAME; mRNA.
DR   EMBL; AY082886; AAL92872.1; -; mRNA.
DR   EMBL; AF281070; AAM69365.1; -; mRNA.
DR   EMBL; AK131407; BAD18554.1; ALT_SEQ; mRNA.
DR   EMBL; BX647812; CAI46013.1; -; mRNA.
DR   EMBL; AC078797; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR   EMBL; CH471052; EAW78257.1; -; Genomic_DNA.
DR   EMBL; CH471052; EAW78259.1; -; Genomic_DNA.
DR   EMBL; CH471052; EAW78262.1; -; Genomic_DNA.
DR   EMBL; CH471052; EAW78263.1; -; Genomic_DNA.
DR   EMBL; CH471052; EAW78264.1; -; Genomic_DNA.
DR   EMBL; CH471052; EAW78265.1; -; Genomic_DNA.
DR   EMBL; CH471052; EAW78266.1; -; Genomic_DNA.
DR   EMBL; CH471052; EAW78267.1; -; Genomic_DNA.
DR   EMBL; AF002816; AAC78443.1; -; mRNA.
DR   EMBL; AF004836; AAC78444.1; ALT_INIT; Genomic_DNA.
DR   EMBL; AF104913; AAC82471.1; ALT_INIT; mRNA.
DR   EMBL; AJ001046; CAA04500.1; -; mRNA.
DR   CCDS; CCDS3259.1; -. [Q04637-1]
DR   CCDS; CCDS3260.1; -. [Q04637-4]
DR   CCDS; CCDS3261.1; -. [Q04637-5]
DR   CCDS; CCDS46970.2; -. [Q04637-7]
DR   CCDS; CCDS54687.1; -. [Q04637-9]
DR   CCDS; CCDS54688.1; -. [Q04637-8]
DR   CCDS; CCDS77866.1; -. [Q04637-3]
DR   PIR; A44453; A44453.
DR   RefSeq; NP_004944.3; NM_004953.4. [Q04637-7]
DR   RefSeq; NP_886553.3; NM_182917.4.
DR   RefSeq; NP_937884.1; NM_198241.2. [Q04637-1]
DR   RefSeq; NP_937885.1; NM_198242.2. [Q04637-5]
DR   PDB; 1LJ2; X-ray; 2.38 A; C/D=172-199.
DR   PDB; 1UG3; X-ray; 2.24 A; A/B=1233-1571.
DR   PDB; 2W97; X-ray; 2.29 A; E/F=609-622.
DR   PDB; 4AZA; X-ray; 2.16 A; B/D=609-620.
DR   PDB; 4F02; X-ray; 2.00 A; C/F=178-203.
DR   PDB; 5EHC; X-ray; 2.40 A; B=609-622.
DR   PDB; 5EI3; X-ray; 1.71 A; B=609-622.
DR   PDB; 5EIR; X-ray; 2.69 A; B=609-622.
DR   PDB; 5T46; X-ray; 1.53 A; B/D=592-653.
DR   PDB; 5ZK5; X-ray; 2.25 A; B=609-623.
DR   PDB; 6ZMW; EM; 3.70 A; g=290-1599.
DR   PDB; 8HUJ; EM; 3.76 A; B=746-992.
DR   PDB; 8J7R; EM; 3.70 A; B=746-992.
DR   PDBsum; 1LJ2; -.
DR   PDBsum; 1UG3; -.
DR   PDBsum; 2W97; -.
DR   PDBsum; 4AZA; -.
DR   PDBsum; 4F02; -.
DR   PDBsum; 5EHC; -.
DR   PDBsum; 5EI3; -.
DR   PDBsum; 5EIR; -.
DR   PDBsum; 5T46; -.
DR   PDBsum; 5ZK5; -.
DR   PDBsum; 6ZMW; -.
DR   PDBsum; 8HUJ; -.
DR   PDBsum; 8J7R; -.
DR   AlphaFoldDB; Q04637; -.
DR   BMRB; Q04637; -.
DR   EMDB; EMD-11302; -.
DR   EMDB; EMD-35041; -.
DR   EMDB; EMD-36046; -.
DR   SMR; Q04637; -.
DR   BioGRID; 108296; 404.
DR   ComplexPortal; CPX-2666; Eukaryotic translation initiation factor 4F, EIF4A1 and EIF4G1 variant.
DR   ComplexPortal; CPX-5634; Eukaryotic translation initiation factor 4F, EIF4A2 and EIF4G1 variant.
DR   CORUM; Q04637; -.
DR   DIP; DIP-1161N; -.
DR   ELM; Q04637; -.
DR   IntAct; Q04637; 105.
DR   MINT; Q04637; -.
DR   STRING; 9606.ENSP00000416255; -.
DR   BindingDB; Q04637; -.
DR   ChEMBL; CHEMBL4523621; -.
DR   MoonProt; Q04637; -.
DR   GlyConnect; 2847; 1 O-GlcNAc glycan (1 site).
DR   GlyCosmos; Q04637; 6 sites, 1 glycan.
DR   GlyGen; Q04637; 12 sites, 1 O-linked glycan (12 sites).
DR   iPTMnet; Q04637; -.
DR   MetOSite; Q04637; -.
DR   PhosphoSitePlus; Q04637; -.
DR   SwissPalm; Q04637; -.
DR   BioMuta; EIF4G1; -.
DR   DMDM; 294862538; -.
DR   EPD; Q04637; -.
DR   jPOST; Q04637; -.
DR   MassIVE; Q04637; -.
DR   MaxQB; Q04637; -.
DR   PaxDb; 9606-ENSP00000416255; -.
DR   PeptideAtlas; Q04637; -.
DR   ProteomicsDB; 20132; -.
DR   ProteomicsDB; 34026; -.
DR   ProteomicsDB; 58250; -. [Q04637-1]
DR   ProteomicsDB; 58251; -. [Q04637-3]
DR   ProteomicsDB; 58252; -. [Q04637-4]
DR   ProteomicsDB; 58253; -. [Q04637-5]
DR   ProteomicsDB; 58254; -. [Q04637-6]
DR   Pumba; Q04637; -.
DR   Antibodypedia; 3406; 709 antibodies from 37 providers.
DR   DNASU; 1981; -.
DR   Ensembl; ENST00000342981.8; ENSP00000343450.4; ENSG00000114867.22. [Q04637-8]
DR   Ensembl; ENST00000346169.7; ENSP00000316879.5; ENSG00000114867.22. [Q04637-1]
DR   Ensembl; ENST00000350481.9; ENSP00000317600.8; ENSG00000114867.22. [Q04637-5]
DR   Ensembl; ENST00000352767.7; ENSP00000338020.4; ENSG00000114867.22. [Q04637-9]
DR   Ensembl; ENST00000382330.7; ENSP00000371767.3; ENSG00000114867.22. [Q04637-9]
DR   Ensembl; ENST00000392537.6; ENSP00000376320.2; ENSG00000114867.22. [Q04637-4]
DR   Ensembl; ENST00000414031.5; ENSP00000391935.1; ENSG00000114867.22. [Q04637-3]
DR   Ensembl; ENST00000424196.5; ENSP00000416255.1; ENSG00000114867.22. [Q04637-9]
DR   Ensembl; ENST00000434061.6; ENSP00000411826.2; ENSG00000114867.22. [Q04637-7]
DR   GeneID; 1981; -.
DR   KEGG; hsa:1981; -.
DR   MANE-Select; ENST00000346169.7; ENSP00000316879.5; NM_198241.3; NP_937884.2.
DR   UCSC; uc003fnp.4; human. [Q04637-1]
DR   AGR; HGNC:3296; -.
DR   CTD; 1981; -.
DR   DisGeNET; 1981; -.
DR   GeneCards; EIF4G1; -.
DR   HGNC; HGNC:3296; EIF4G1.
DR   HPA; ENSG00000114867; Tissue enhanced (skeletal).
DR   MalaCards; EIF4G1; -.
DR   MIM; 600495; gene.
DR   MIM; 614251; phenotype.
DR   neXtProt; NX_Q04637; -.
DR   OpenTargets; ENSG00000114867; -.
DR   Orphanet; 411602; Hereditary late-onset Parkinson disease.
DR   PharmGKB; PA27722; -.
DR   VEuPathDB; HostDB:ENSG00000114867; -.
DR   eggNOG; KOG0401; Eukaryota.
DR   GeneTree; ENSGT00940000154648; -.
DR   HOGENOM; CLU_001519_2_0_1; -.
DR   InParanoid; Q04637; -.
DR   OMA; PRGGPNM; -.
DR   OrthoDB; 92033at2759; -.
DR   PhylomeDB; Q04637; -.
DR   TreeFam; TF101527; -.
DR   PathwayCommons; Q04637; -.
DR   Reactome; R-HSA-1169408; ISG15 antiviral mechanism.
DR   Reactome; R-HSA-156827; L13a-mediated translational silencing of Ceruloplasmin expression.
DR   Reactome; R-HSA-166208; mTORC1-mediated signalling.
DR   Reactome; R-HSA-429947; Deadenylation of mRNA.
DR   Reactome; R-HSA-450408; AUF1 (hnRNP D0) binds and destabilizes mRNA.
DR   Reactome; R-HSA-72649; Translation initiation complex formation.
DR   Reactome; R-HSA-72662; Activation of the mRNA upon binding of the cap-binding complex and eIFs, and subsequent binding to 43S.
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   Reactome; R-HSA-9010553; Regulation of expression of SLITs and ROBOs.
DR   Reactome; R-HSA-975956; Nonsense Mediated Decay (NMD) independent of the Exon Junction Complex (EJC).
DR   Reactome; R-HSA-975957; Nonsense Mediated Decay (NMD) enhanced by the Exon Junction Complex (EJC).
DR   Reactome; R-HSA-9820841; M-decay: degradation of maternal mRNAs by maternally stored factors.
DR   Reactome; R-HSA-9820865; Z-decay: degradation of maternal mRNAs by zygotically expressed factors.
DR   SignaLink; Q04637; -.
DR   SIGNOR; Q04637; -.
DR   BioGRID-ORCS; 1981; 612 hits in 1167 CRISPR screens.
DR   ChiTaRS; EIF4G1; human.
DR   EvolutionaryTrace; Q04637; -.
DR   GeneWiki; Eukaryotic_translation_initiation_factor_4_gamma; -.
DR   GenomeRNAi; 1981; -.
DR   Pharos; Q04637; Tbio.
DR   PRO; PR:Q04637; -.
DR   Proteomes; UP000005640; Chromosome 3.
DR   RNAct; Q04637; Protein.
DR   Bgee; ENSG00000114867; Expressed in gastrocnemius and 206 other cell types or tissues.
DR   ExpressionAtlas; Q04637; baseline and differential.
DR   Genevisible; Q04637; HS.
DR   GO; GO:0005737; C:cytoplasm; IDA:AgBase.
DR   GO; GO:0010494; C:cytoplasmic stress granule; IDA:UniProtKB.
DR   GO; GO:0005829; C:cytosol; IDA:HPA.
DR   GO; GO:0016281; C:eukaryotic translation initiation factor 4F complex; IDA:ParkinsonsUK-UCL.
DR   GO; GO:0016020; C:membrane; HDA:UniProtKB.
DR   GO; GO:0005634; C:nucleus; IDA:UniProtKB.
DR   GO; GO:0098794; C:postsynapse; IEA:Ensembl.
DR   GO; GO:0005840; C:ribosome; IMP:ParkinsonsUK-UCL.
DR   GO; GO:0005524; F:ATP binding; IDA:ParkinsonsUK-UCL.
DR   GO; GO:0008190; F:eukaryotic initiation factor 4E binding; IDA:AgBase.
DR   GO; GO:0042802; F:identical protein binding; IPI:IntAct.
DR   GO; GO:0060090; F:molecular adaptor activity; TAS:ParkinsonsUK-UCL.
DR   GO; GO:0003729; F:mRNA binding; IDA:ParkinsonsUK-UCL.
DR   GO; GO:0003723; F:RNA binding; HDA:UniProtKB.
DR   GO; GO:0008135; F:translation factor activity, RNA binding; IMP:ParkinsonsUK-UCL.
DR   GO; GO:0003743; F:translation initiation factor activity; IDA:UniProtKB.
DR   GO; GO:0031369; F:translation initiation factor binding; TAS:ParkinsonsUK-UCL.
DR   GO; GO:0001662; P:behavioral fear response; IEA:Ensembl.
DR   GO; GO:0002191; P:cap-dependent translational initiation; TAS:ParkinsonsUK-UCL.
DR   GO; GO:0031669; P:cellular response to nutrient levels; IMP:ParkinsonsUK-UCL.
DR   GO; GO:0097009; P:energy homeostasis; IMP:ParkinsonsUK-UCL.
DR   GO; GO:0030324; P:lung development; IEA:Ensembl.
DR   GO; GO:0009059; P:macromolecule biosynthetic process; IGI:ParkinsonsUK-UCL.
DR   GO; GO:0035278; P:miRNA-mediated gene silencing by inhibition of translation; IDA:ParkinsonsUK-UCL.
DR   GO; GO:0010507; P:negative regulation of autophagy; IMP:ParkinsonsUK-UCL.
DR   GO; GO:0010801; P:negative regulation of peptidyl-threonine phosphorylation; IMP:ParkinsonsUK-UCL.
DR   GO; GO:0030182; P:neuron differentiation; IEA:Ensembl.
DR   GO; GO:0030307; P:positive regulation of cell growth; IMP:ParkinsonsUK-UCL.
DR   GO; GO:1905537; P:positive regulation of eukaryotic translation initiation factor 4F complex assembly; IMP:ParkinsonsUK-UCL.
DR   GO; GO:1900087; P:positive regulation of G1/S transition of mitotic cell cycle; IMP:ParkinsonsUK-UCL.
DR   GO; GO:1905612; P:positive regulation of mRNA cap binding; IDA:ParkinsonsUK-UCL.
DR   GO; GO:0045666; P:positive regulation of neuron differentiation; IEA:Ensembl.
DR   GO; GO:0033138; P:positive regulation of peptidyl-serine phosphorylation; IMP:ParkinsonsUK-UCL.
DR   GO; GO:1904377; P:positive regulation of protein localization to cell periphery; IGI:ParkinsonsUK-UCL.
DR   GO; GO:0051247; P:positive regulation of protein metabolic process; IMP:ParkinsonsUK-UCL.
DR   GO; GO:0036493; P:positive regulation of translation in response to endoplasmic reticulum stress; IMP:UniProtKB.
DR   GO; GO:0080135; P:regulation of cellular response to stress; TAS:ParkinsonsUK-UCL.
DR   GO; GO:1905606; P:regulation of presynapse assembly; IGI:ARUK-UCL.
DR   GO; GO:0006446; P:regulation of translational initiation; IMP:UniProtKB.
DR   GO; GO:0045471; P:response to ethanol; IEA:Ensembl.
DR   GO; GO:0006412; P:translation; IMP:ParkinsonsUK-UCL.
DR   GO; GO:0006413; P:translational initiation; IDA:UniProtKB.
DR   CDD; cd11559; W2_eIF4G1_like; 1.
DR   DisProt; DP02398; -.
DR   Gene3D; 1.25.40.180; -; 3.
DR   InterPro; IPR016024; ARM-type_fold.
DR   InterPro; IPR045208; IF4G.
DR   InterPro; IPR003891; Initiation_fac_eIF4g_MI.
DR   InterPro; IPR003890; MIF4G-like_typ-3.
DR   InterPro; IPR003307; W2_domain.
DR   PANTHER; PTHR23253; EUKARYOTIC TRANSLATION INITIATION FACTOR 4 GAMMA; 1.
DR   PANTHER; PTHR23253:SF10; EUKARYOTIC TRANSLATION INITIATION FACTOR 4 GAMMA 1; 1.
DR   Pfam; PF02847; MA3; 1.
DR   Pfam; PF02854; MIF4G; 1.
DR   Pfam; PF02020; W2; 1.
DR   SMART; SM00515; eIF5C; 1.
DR   SMART; SM00544; MA3; 1.
DR   SMART; SM00543; MIF4G; 1.
DR   SUPFAM; SSF48371; ARM repeat; 3.
DR   PROSITE; PS51366; MI; 1.
DR   PROSITE; PS51363; W2; 1.
PE   1: Evidence at protein level;
KW   3D-structure; Acetylation; Alternative initiation; Alternative splicing;
KW   Cytoplasm; Disease variant; Host-virus interaction; Initiation factor;
KW   Methylation; Neurodegeneration; Nucleus; Parkinson disease; Parkinsonism;
KW   Phosphoprotein; Protein biosynthesis; Reference proteome; RNA-binding;
KW   Translation regulation; Translational shunt.
FT   CHAIN           1..1599
FT                   /note="Eukaryotic translation initiation factor 4 gamma 1"
FT                   /id="PRO_0000007786"
FT   DOMAIN          565..792
FT                   /note="MIF4G"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00698"
FT   DOMAIN          1241..1363
FT                   /note="MI"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00698"
FT   DOMAIN          1433..1599
FT                   /note="W2"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00695"
FT   REGION          1..77
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          166..222
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          172..200
FT                   /note="PABPC1-binding"
FT   REGION          234..319
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          332..600
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          607..618
FT                   /note="EIF4E-binding"
FT   REGION          667..713
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          682..1085
FT                   /note="eIF3/EIF4A-binding"
FT   REGION          731..757
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          1024..1227
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          1450..1599
FT                   /note="EIF4A-binding"
FT   REGION          1585..1599
FT                   /note="Necessary but not sufficient for MKNK1-binding"
FT   COMPBIAS        7..26
FT                   /note="Pro residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        30..67
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        174..190
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        198..218
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        255..273
FT                   /note="Pro residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        285..303
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        335..350
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        377..394
FT                   /note="Pro residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        434..451
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        453..471
FT                   /note="Acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        490..504
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        564..586
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        1059..1087
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        1112..1141
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        1142..1223
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   SITE            674..675
FT                   /note="Cleavage; by foot-and-mouth disease virus leader
FT                   protease"
FT   SITE            681..682
FT                   /note="Cleavage; by enterovirus/rhinovirus protease 2A"
FT   MOD_RES         15
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0000250|UniProtKB:Q6NZJ6"
FT   MOD_RES         73
FT                   /note="Omega-N-methylarginine"
FT                   /evidence="ECO:0007744|PubMed:24129315"
FT   MOD_RES         110
FT                   /note="Omega-N-methylarginine"
FT                   /evidence="ECO:0007744|PubMed:24129315"
FT   MOD_RES         207
FT                   /note="Phosphothreonine"
FT                   /evidence="ECO:0007744|PubMed:18669648,
FT                   ECO:0007744|PubMed:23186163"
FT   MOD_RES         223
FT                   /note="Phosphothreonine"
FT                   /evidence="ECO:0007744|PubMed:18669648"
FT   MOD_RES         314
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0007744|PubMed:24275569"
FT   MOD_RES         602
FT                   /note="N6-acetyllysine"
FT                   /evidence="ECO:0000250|UniProtKB:Q6NZJ6"
FT   MOD_RES         647
FT                   /note="Phosphothreonine"
FT                   /evidence="ECO:0007744|PubMed:18669648,
FT                   ECO:0007744|PubMed:23186163"
FT   MOD_RES         685
FT                   /note="Omega-N-methylarginine"
FT                   /evidence="ECO:0007744|PubMed:24129315"
FT   MOD_RES         694
FT                   /note="Omega-N-methylarginine"
FT                   /evidence="ECO:0007744|PubMed:24129315"
FT   MOD_RES         1028
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0007744|PubMed:20068231,
FT                   ECO:0007744|PubMed:21406692, ECO:0007744|PubMed:23186163"
FT   MOD_RES         1032
FT                   /note="Omega-N-methylarginine"
FT                   /evidence="ECO:0007744|PubMed:24129315"
FT   MOD_RES         1042
FT                   /note="Omega-N-methylarginine"
FT                   /evidence="ECO:0007744|PubMed:24129315"
FT   MOD_RES         1077
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0007744|PubMed:23186163"
FT   MOD_RES         1092
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0007744|PubMed:17924679,
FT                   ECO:0007744|PubMed:18669648, ECO:0007744|PubMed:20068231,
FT                   ECO:0007744|PubMed:21406692, ECO:0007744|PubMed:23186163"
FT   MOD_RES         1095
FT                   /note="N6-acetyllysine"
FT                   /evidence="ECO:0007744|PubMed:19608861"
FT   MOD_RES         1145
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0007744|PubMed:21406692,
FT                   ECO:0007744|PubMed:23186163"
FT   MOD_RES         1147
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0007744|PubMed:21406692,
FT                   ECO:0007744|PubMed:23186163"
FT   MOD_RES         1185
FT                   /note="Phosphoserine; by PKC/PRKCA"
FT                   /evidence="ECO:0000269|PubMed:21576361,
FT                   ECO:0007744|PubMed:20068231, ECO:0007744|PubMed:21406692,
FT                   ECO:0007744|PubMed:23186163"
FT   MOD_RES         1187
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0007744|PubMed:20068231,
FT                   ECO:0007744|PubMed:21406692, ECO:0007744|PubMed:23186163"
FT   MOD_RES         1194
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0007744|PubMed:23186163"
FT   MOD_RES         1209
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0007744|PubMed:18669648,
FT                   ECO:0007744|PubMed:20068231, ECO:0007744|PubMed:21406692,
FT                   ECO:0007744|PubMed:23186163"
FT   MOD_RES         1211
FT                   /note="Phosphothreonine"
FT                   /evidence="ECO:0007744|PubMed:20068231,
FT                   ECO:0007744|PubMed:21406692"
FT   MOD_RES         1231
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0007744|PubMed:16964243,
FT                   ECO:0007744|PubMed:17081983, ECO:0007744|PubMed:20068231,
FT                   ECO:0007744|PubMed:21406692, ECO:0007744|PubMed:23186163"
FT   MOD_RES         1238
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0007744|PubMed:23186163"
FT   MOD_RES         1596
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0007744|PubMed:20068231,
FT                   ECO:0007744|PubMed:21406692, ECO:0007744|PubMed:23186163"
FT   VAR_SEQ         1..196
FT                   /note="Missing (in isoform E and isoform 7)"
FT                   /evidence="ECO:0000303|PubMed:1429670"
FT                   /id="VSP_018723"
FT   VAR_SEQ         1..164
FT                   /note="Missing (in isoform D)"
FT                   /evidence="ECO:0000305"
FT                   /id="VSP_018722"
FT   VAR_SEQ         1..87
FT                   /note="Missing (in isoform C)"
FT                   /evidence="ECO:0000303|PubMed:9418880"
FT                   /id="VSP_018721"
FT   VAR_SEQ         1..40
FT                   /note="Missing (in isoform B)"
FT                   /evidence="ECO:0000303|PubMed:9857202"
FT                   /id="VSP_018720"
FT   VAR_SEQ         48
FT                   /note="R -> RQGGFRSL (in isoform 9)"
FT                   /evidence="ECO:0000305"
FT                   /id="VSP_047396"
FT   VAR_SEQ         696
FT                   /note="P -> PQ (in isoform 7 and isoform 8)"
FT                   /evidence="ECO:0000303|PubMed:12052860,
FT                   ECO:0000303|PubMed:1429670, ECO:0000303|PubMed:9372926,
FT                   ECO:0000303|Ref.12"
FT                   /id="VSP_047397"
FT   VARIANT         71
FT                   /note="P -> S (in dbSNP:rs113810947)"
FT                   /evidence="ECO:0000269|PubMed:21907011"
FT                   /id="VAR_066571"
FT   VARIANT         161
FT                   /note="T -> A (in dbSNP:rs13319149)"
FT                   /evidence="ECO:0000269|PubMed:12052860,
FT                   ECO:0000269|PubMed:17974005, ECO:0000269|PubMed:21907011,
FT                   ECO:0000269|PubMed:9372926, ECO:0000269|PubMed:9755181"
FT                   /id="VAR_061147"
FT   VARIANT         201
FT                   /note="R -> H (found in a patient with Rett syndrome-like
FT                   phenotype; uncertain significance; dbSNP:rs34838305)"
FT                   /evidence="ECO:0000269|PubMed:26740508"
FT                   /id="VAR_079031"
FT   VARIANT         311
FT                   /note="Y -> C (in dbSNP:rs16858632)"
FT                   /evidence="ECO:0000269|PubMed:21907011"
FT                   /id="VAR_055704"
FT   VARIANT         432
FT                   /note="M -> V (in dbSNP:rs2178403)"
FT                   /evidence="ECO:0000269|PubMed:12052860,
FT                   ECO:0000269|PubMed:1429670, ECO:0000269|PubMed:21907011,
FT                   ECO:0000269|PubMed:9372926, ECO:0007744|PubMed:19413330"
FT                   /id="VAR_063040"
FT   VARIANT         466..468
FT                   /note="Missing"
FT                   /evidence="ECO:0000269|PubMed:21907011"
FT                   /id="VAR_066572"
FT   VARIANT         502
FT                   /note="A -> V (in PARK18; dbSNP:rs111290936)"
FT                   /evidence="ECO:0000269|PubMed:21907011"
FT                   /id="VAR_066573"
FT   VARIANT         686
FT                   /note="G -> C (found in patients with Parkinson disease;
FT                   uncertain significance; dbSNP:rs112019125)"
FT                   /evidence="ECO:0000269|PubMed:21907011"
FT                   /id="VAR_066574"
FT   VARIANT         696
FT                   /note="P -> L (in a colorectal cancer sample; somatic
FT                   mutation; dbSNP:rs754755344)"
FT                   /evidence="ECO:0000269|PubMed:16959974"
FT                   /id="VAR_036117"
FT   VARIANT         806
FT                   /note="I -> V (in dbSNP:rs62287499)"
FT                   /evidence="ECO:0000269|PubMed:21907011"
FT                   /id="VAR_066575"
FT   VARIANT         829
FT                   /note="T -> S (in dbSNP:rs111500185)"
FT                   /evidence="ECO:0000269|PubMed:21907011"
FT                   /id="VAR_066576"
FT   VARIANT         1164
FT                   /note="S -> R (found in a patient with Parkinson disease;
FT                   uncertain significance; dbSNP:rs113169049)"
FT                   /evidence="ECO:0000269|PubMed:21907011"
FT                   /id="VAR_066577"
FT   VARIANT         1197
FT                   /note="R -> W (found in a patient with Parkinson disease;
FT                   uncertain significance; dbSNP:rs113388242)"
FT                   /evidence="ECO:0000269|PubMed:21907011"
FT                   /id="VAR_066578"
FT   VARIANT         1205
FT                   /note="R -> H (in PARK18; dbSNP:rs112176450)"
FT                   /evidence="ECO:0000269|PubMed:21907011"
FT                   /id="VAR_066579"
FT   VARIANT         1229
FT                   /note="P -> A (in dbSNP:rs35629949)"
FT                   /evidence="ECO:0000269|PubMed:21907011"
FT                   /id="VAR_061148"
FT   VARIANT         1233
FT                   /note="L -> P (in dbSNP:rs2230570)"
FT                   /evidence="ECO:0000269|PubMed:21907011"
FT                   /id="VAR_055705"
FT   VARIANT         1257
FT                   /note="N -> S (in dbSNP:rs73053766)"
FT                   /evidence="ECO:0000269|PubMed:21907011"
FT                   /id="VAR_066580"
FT   MUTAGEN         174..178
FT                   /note="KRERK->AAAAA: Loss of PABPC1 binding; when
FT                   associated with 184-AAAA-187."
FT                   /evidence="ECO:0000269|PubMed:10996799"
FT   MUTAGEN         180
FT                   /note="I->A: Loss of PABPC1 binding."
FT                   /evidence="ECO:0000269|PubMed:12086624"
FT   MUTAGEN         182
FT                   /note="I->A: Loss of PABPC1 binding."
FT                   /evidence="ECO:0000269|PubMed:12086624"
FT   MUTAGEN         184..187
FT                   /note="DPNQ->AAAA: Loss of PABPC1 binding; when associated
FT                   with 174-AAAAA-178."
FT   MUTAGEN         192
FT                   /note="I->A: Loss of PABPC1 binding."
FT                   /evidence="ECO:0000269|PubMed:12086624"
FT   MUTAGEN         196
FT                   /note="I->A: Loss of PABPC1 binding."
FT                   /evidence="ECO:0000269|PubMed:12086624"
FT   MUTAGEN         612
FT                   /note="Y->A,F: Abolishes binding to EIF4E."
FT                   /evidence="ECO:0000269|PubMed:7651417"
FT   MUTAGEN         617..618
FT                   /note="LL->AA: Abolishes binding to EIF4E."
FT                   /evidence="ECO:0000269|PubMed:7651417"
FT   MUTAGEN         682
FT                   /note="G->A,V,W,R,E: Reduced cleavage by protease 2A from
FT                   human rhinovirus 2."
FT                   /evidence="ECO:0000269|PubMed:8961935"
FT   MUTAGEN         768
FT                   /note="L->A: Abolishes binding to EIF4A; when associated
FT                   with A-770 and A-775."
FT                   /evidence="ECO:0000269|PubMed:9372926"
FT   MUTAGEN         771
FT                   /note="L->A: Abolishes binding to EIF4A; when associated
FT                   with A-767 and A-775."
FT                   /evidence="ECO:0000269|PubMed:9372926"
FT   MUTAGEN         776
FT                   /note="F->A: Abolishes binding to EIF4A; when associated
FT                   with A-767 and A-770."
FT                   /evidence="ECO:0000269|PubMed:9372926"
FT   MUTAGEN         842..843
FT                   /note="LL->AA: Abolishes binding to EIF4A; when associated
FT                   with A-850 and K-851."
FT                   /evidence="ECO:0000269|PubMed:9372926"
FT   MUTAGEN         851..852
FT                   /note="FE->AK: Abolishes binding to EIF4A; when associated
FT                   with A-841 and A-842."
FT                   /evidence="ECO:0000269|PubMed:9372926"
FT   MUTAGEN         896
FT                   /note="L->A: Abolishes binding to EIF4A; when associated
FT                   with A-92 and A-95."
FT                   /evidence="ECO:0000269|PubMed:9372926"
FT   MUTAGEN         902
FT                   /note="I->A: Abolishes binding to EIF4A; when associated
FT                   with A-895 and A-95."
FT                   /evidence="ECO:0000269|PubMed:9372926"
FT   MUTAGEN         905
FT                   /note="L->A: Abolishes binding to EIF4A; when associated
FT                   with A-895 and A-92."
FT                   /evidence="ECO:0000269|PubMed:9372926"
FT   MUTAGEN         974
FT                   /note="R->A: Abolishes binding to EIF4A; when associated
FT                   with A-976."
FT                   /evidence="ECO:0000269|PubMed:9372926"
FT   MUTAGEN         977
FT                   /note="F->A: Abolishes binding to EIF4A; when associated
FT                   with A-973."
FT                   /evidence="ECO:0000269|PubMed:9372926"
FT   MUTAGEN         985
FT                   /note="L->A: Slightly reduced binding to EIF4A; when
FT                   associated with A-989."
FT                   /evidence="ECO:0000269|PubMed:9372926"
FT   MUTAGEN         990
FT                   /note="W->A: Slightly reduced binding to EIF4A; when
FT                   associated with A-984."
FT                   /evidence="ECO:0000269|PubMed:9372926"
FT   CONFLICT        30
FT                   /note="P -> R (in Ref. 9; AAC78443)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        138
FT                   /note="F -> L (in Ref. 5; AAL92872/AAM69365)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        149
FT                   /note="Q -> R (in Ref. 5; AAL92872/AAM69365)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        214
FT                   /note="G -> S (in Ref. 1; BAA02185)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        462
FT                   /note="E -> D (in Ref. 1; BAA02185)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        468
FT                   /note="A -> V (in Ref. 1; BAA02185)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        474
FT                   /note="A -> G (in Ref. 1; BAA02185)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        479
FT                   /note="G -> R (in Ref. 1; BAA02185)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        604
FT                   /note="L -> P (in Ref. 1; BAA02185, 5; AAL92872/AAM69365
FT                   and 10; AAC82471)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        625..626
FT                   /note="AS -> CQ (in Ref. 1; BAA02185)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        693
FT                   /note="P -> A (in Ref. 1; BAA02185)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        696
FT                   /note="P -> A (in Ref. 1; BAA02185)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        764
FT                   /note="V -> W (in Ref. 1; BAA02185)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        878
FT                   /note="G -> E (in Ref. 1; BAA02185)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        894
FT                   /note="R -> C (in Ref. 1; BAA02185)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        1104
FT                   /note="K -> Q (in Ref. 1; BAA02185)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        1121
FT                   /note="N -> I (in Ref. 1; BAA02185)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        1185
FT                   /note="S -> T (in Ref. 1; BAA02185)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        1384
FT                   /note="C -> Y (in Ref. 6; CAI46013)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        1472
FT                   /note="Missing (in Ref. 1; BAA02185)"
FT                   /evidence="ECO:0000305"
FT   STRAND          181..183
FT                   /evidence="ECO:0007829|PDB:1LJ2"
FT   HELIX           185..187
FT                   /evidence="ECO:0007829|PDB:4F02"
FT   HELIX           193..197
FT                   /evidence="ECO:0007829|PDB:4F02"
FT   HELIX           614..618
FT                   /evidence="ECO:0007829|PDB:5T46"
FT   TURN            619..622
FT                   /evidence="ECO:0007829|PDB:5T46"
FT   HELIX           624..627
FT                   /evidence="ECO:0007829|PDB:5T46"
FT   TURN            637..639
FT                   /evidence="ECO:0007829|PDB:5T46"
FT   HELIX           1234..1256
FT                   /evidence="ECO:0007829|PDB:1UG3"
FT   HELIX           1259..1267
FT                   /evidence="ECO:0007829|PDB:1UG3"
FT   HELIX           1272..1274
FT                   /evidence="ECO:0007829|PDB:1UG3"
FT   HELIX           1275..1286
FT                   /evidence="ECO:0007829|PDB:1UG3"
FT   TURN            1287..1289
FT                   /evidence="ECO:0007829|PDB:1UG3"
FT   HELIX           1291..1306
FT                   /evidence="ECO:0007829|PDB:1UG3"
FT   HELIX           1312..1329
FT                   /evidence="ECO:0007829|PDB:1UG3"
FT   TURN            1330..1332
FT                   /evidence="ECO:0007829|PDB:1UG3"
FT   HELIX           1336..1344
FT                   /evidence="ECO:0007829|PDB:1UG3"
FT   HELIX           1345..1348
FT                   /evidence="ECO:0007829|PDB:1UG3"
FT   HELIX           1355..1362
FT                   /evidence="ECO:0007829|PDB:1UG3"
FT   TURN            1363..1365
FT                   /evidence="ECO:0007829|PDB:1UG3"
FT   HELIX           1366..1369
FT                   /evidence="ECO:0007829|PDB:1UG3"
FT   HELIX           1372..1387
FT                   /evidence="ECO:0007829|PDB:1UG3"
FT   HELIX           1389..1398
FT                   /evidence="ECO:0007829|PDB:1UG3"
FT   HELIX           1403..1405
FT                   /evidence="ECO:0007829|PDB:1UG3"
FT   HELIX           1413..1419
FT                   /evidence="ECO:0007829|PDB:1UG3"
FT   HELIX           1423..1425
FT                   /evidence="ECO:0007829|PDB:1UG3"
FT   HELIX           1439..1452
FT                   /evidence="ECO:0007829|PDB:1UG3"
FT   HELIX           1457..1467
FT                   /evidence="ECO:0007829|PDB:1UG3"
FT   HELIX           1470..1473
FT                   /evidence="ECO:0007829|PDB:1UG3"
FT   HELIX           1476..1489
FT                   /evidence="ECO:0007829|PDB:1UG3"
FT   STRAND          1494..1496
FT                   /evidence="ECO:0007829|PDB:1UG3"
FT   HELIX           1501..1514
FT                   /evidence="ECO:0007829|PDB:1UG3"
FT   HELIX           1518..1534
FT                   /evidence="ECO:0007829|PDB:1UG3"
FT   HELIX           1541..1551
FT                   /evidence="ECO:0007829|PDB:1UG3"
FT   HELIX           1557..1563
FT                   /evidence="ECO:0007829|PDB:1UG3"
FT   INIT_MET        Q04637-4:1
FT                   /note="Removed"
FT                   /evidence="ECO:0007744|PubMed:22814378"
FT   MOD_RES         Q04637-4:2
FT                   /note="N-acetylmethionine"
FT                   /evidence="ECO:0007744|PubMed:22814378"
FT   MOD_RES         Q04637-7:489
FT                   /note="Omega-N-methylarginine"
FT                   /evidence="ECO:0007744|PubMed:24129315"
FT   MOD_RES         Q04637-7:498
FT                   /note="Omega-N-methylarginine"
FT                   /evidence="ECO:0007744|PubMed:24129315"
FT   MOD_RES         Q04637-7:509
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0007744|PubMed:23186163"
FT   MOD_RES         Q04637-8:685
FT                   /note="Omega-N-methylarginine"
FT                   /evidence="ECO:0007744|PubMed:24129315"
FT   MOD_RES         Q04637-8:694
FT                   /note="Omega-N-methylarginine"
FT                   /evidence="ECO:0007744|PubMed:24129315"
FT   MOD_RES         Q04637-8:705
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0007744|PubMed:23186163"
SQ   SEQUENCE   1599 AA;  175491 MW;  324088B60863DA34 CRC64;
     MNKAPQSTGP PPAPSPGLPQ PAFPPGQTAP VVFSTPQATQ MNTPSQPRQH FYPSRAQPPS
     SAASRVQSAA PARPGPAAHV YPAGSQVMMI PSQISYPASQ GAYYIPGQGR STYVVPTQQY
     PVQPGAPGFY PGASPTEFGT YAGAYYPAQG VQQFPTGVAP TPVLMNQPPQ IAPKRERKTI
     RIRDPNQGGK DITEEIMSGA RTASTPTPPQ TGGGLEPQAN GETPQVAVIV RPDDRSQGAI
     IADRPGLPGP EHSPSESQPS SPSPTPSPSP VLEPGSEPNL AVLSIPGDTM TTIQMSVEES
     TPISRETGEP YRLSPEPTPL AEPILEVEVT LSKPVPESEF SSSPLQAPTP LASHTVEIHE
     PNGMVPSEDL EPEVESSPEL APPPACPSES PVPIAPTAQP EELLNGAPSP PAVDLSPVSE
     PEEQAKEVTA SMAPPTIPSA TPATAPSATS PAQEEEMEEE EEEEEGEAGE AGEAESEKGG
     EELLPPESTP IPANLSQNLE AAAATQVAVS VPKRRRKIKE LNKKEAVGDL LDAFKEANPA
     VPEVENQPPA GSNPGPESEG SGVPPRPEEA DETWDSKEDK IHNAENIQPG EQKYEYKSDQ
     WKPLNLEEKK RYDREFLLGF QFIFASMQKP EGLPHISDVV LDKANKTPLR PLDPTRLQGI
     NCGPDFTPSF ANLGRTTLST RGPPRGGPGG ELPRGPAGLG PRRSQQGPRK EPRKIIATVL
     MTEDIKLNKA EKAWKPSSKR TAADKDRGEE DADGSKTQDL FRRVRSILNK LTPQMFQQLM
     KQVTQLAIDT EERLKGVIDL IFEKAISEPN FSVAYANMCR CLMALKVPTT EKPTVTVNFR
     KLLLNRCQKE FEKDKDDDEV FEKKQKEMDE AATAEERGRL KEELEEARDI ARRRSLGNIK
     FIGELFKLKM LTEAIMHDCV VKLLKNHDEE SLECLCRLLT TIGKDLDFEK AKPRMDQYFN
     QMEKIIKEKK TSSRIRFMLQ DVLDLRGSNW VPRRGDQGPK TIDQIHKEAE MEEHREHIKV
     QQLMAKGSDK RRGGPPGPPI SRGLPLVDDG GWNTVPISKG SRPIDTSRLT KITKPGSIDS
     NNQLFAPGGR LSWGKGSSGG SGAKPSDAAS EAARPATSTL NRFSALQQAV PTESTDNRRV
     VQRSSLSRER GEKAGDRGDR LERSERGGDR GDRLDRARTP ATKRSFSKEV EERSRERPSQ
     PEGLRKAASL TEDRDRGRDA VKREAALPPV SPLKAALSEE ELEKKSKAII EEYLHLNDMK
     EAVQCVQELA SPSLLFIFVR HGVESTLERS AIAREHMGQL LHQLLCAGHL STAQYYQGLY
     EILELAEDME IDIPHVWLYL AELVTPILQE GGVPMGELFR EITKPLRPLG KAASLLLEIL
     GLLCKSMGPK KVGTLWREAG LSWKEFLPEG QDIGAFVAEQ KVEYTLGEES EAPGQRALPS
     EELNRQLEKL LKEGSSNQRV FDWIEANLSE QQIVSNTLVR ALMTAVCYSA IIFETPLRVD
     VAVLKARAKL LQKYLCDEQK ELQALYALQA LVVTLEQPPN LLRMFFDALY DEDVVKEDAF
     YSWESSKDPA EQQGKGVALK SVTAFFKWLR EAEEESDHN
//
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