IF4G1_HUMAN
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 03-AUG-2022, entry version 234.
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 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 [33]
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 [34]
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 [35]
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 [36]
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 [37]
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 [38]
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 [39]
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 [40]
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 [41]
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 [42]
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 [43]
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 [44]
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 [45]
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 [46]
RP INTERACTION WITH HNRPD, 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 [47]
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 [48]
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 [49]
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 [50]
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 [51]
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 [52]
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 [53]
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. As a
CC member of the eIF4F complex, required for endoplasmic reticulum stress-
CC induced ATF4 mRNA translation (PubMed:29062139).
CC {ECO:0000269|PubMed:29062139}.
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 Interacts with eIF3, mutually exclusive with EIF4A1 or EIFA2, EIF4E and
CC through its N-terminus with PAPBC1. Interacts through its C-terminus
CC with the serine/threonine kinases MKNK1, and with MKNK2. Appears to act
CC as a scaffold protein, holding these enzymes in place to phosphorylate
CC EIF4E. Non-phosphorylated EIF4EBP1 competes with EIF4G1/EIF4G3 to
CC interact with EIF4E; insulin stimulated MAP-kinase (MAPK1 and MAPK3)
CC phosphorylation of EIF4EBP1 causes dissociation of the complex allowing
CC EIF4G1/EIF4G3 to bind and consequent initiation of translation.
CC EIF4G1/EIF4G3 interacts with PABPC1 to bring about circularization of
CC the mRNA. Rapamycin can attenuate insulin stimulation mediated by
CC FKBPs. Interacts with EIF4E3. Interacts with CIRBP and MIF4GD.
CC Interacts with RBM4. Interacts with HNRNPD/AUF1; the interaction
CC requires RNA. Directly interacts with EIF4G1 in an RNA-independent
CC manner (PubMed:22872150). {ECO:0000269|PubMed:10970864,
CC ECO:0000269|PubMed:10996799, ECO:0000269|PubMed:11154262,
CC ECO:0000269|PubMed:12086624, ECO:0000269|PubMed:16513844,
CC ECO:0000269|PubMed:17284590, ECO:0000269|PubMed:18025107,
CC ECO:0000269|PubMed:22872150, ECO:0000269|PubMed:24423872,
CC ECO:0000269|PubMed:7651417, ECO:0000269|PubMed:7935836,
CC ECO:0000269|PubMed:8521827, ECO:0000269|PubMed:9372926,
CC ECO:0000269|PubMed:9755181, 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 -!- 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, 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};
CC ---------------------------------------------------------------------------
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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 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 AlphaFoldDB; Q04637; -.
DR BMRB; Q04637; -.
DR SMR; Q04637; -.
DR BioGRID; 108296; 228.
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; 100.
DR MINT; Q04637; -.
DR STRING; 9606.ENSP00000416255; -.
DR BindingDB; Q04637; -.
DR ChEMBL; CHEMBL4523621; -.
DR MoonProt; Q04637; -.
DR GlyConnect; 2847; 1 O-Linked glycan (1 site).
DR GlyGen; Q04637; 6 sites, 1 O-linked glycan (6 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; Q04637; -.
DR PeptideAtlas; Q04637; -.
DR PRIDE; 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 Antibodypedia; 3406; 624 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 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 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 SignaLink; Q04637; -.
DR SIGNOR; Q04637; -.
DR BioGRID-ORCS; 1981; 581 hits in 1087 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 204 other 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; IEA:UniProtKB-SubCell.
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; IMP:ParkinsonsUK-UCL.
DR GO; GO:0005844; C:polysome; IMP:ParkinsonsUK-UCL.
DR GO; GO:0098794; C:postsynapse; IEA:Ensembl.
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; IBA:GO_Central.
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:0034645; P:cellular macromolecule biosynthetic process; IGI: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: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:1901215; P:negative regulation of neuron death; TAS: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:0010942; P:positive regulation of cell death; IGI:ParkinsonsUK-UCL.
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: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:0060964; P:regulation of miRNA-mediated gene silencing; TAS:ParkinsonsUK-UCL.
DR GO; GO:1905696; P:regulation of polysome binding; IMP:ParkinsonsUK-UCL.
DR GO; GO:1905606; P:regulation of presynapse assembly; IGI:ParkinsonsUK-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; TAS:ParkinsonsUK-UCL.
DR DisProt; DP02398; -.
DR InterPro; IPR016024; ARM-type_fold.
DR InterPro; IPR037584; EIF4G1.
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; PTHR23253; 1.
DR PANTHER; PTHR23253:SF10; PTHR23253:SF10; 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; SSF48371; 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; 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; unknown pathological significance;
FT 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 unknown pathological 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 unknown pathological 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 unknown pathological 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
