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Eukaryotic translation initiation factor 4 gamma 1 (eIF-4-gamma 1) (eIF-4G 1) (eIF-4G1) (p220)

 IF4G1_HUMAN             Reviewed;        1599 AA.
Q04637; D3DNT2; D3DNT4; D3DNT5; E9PFM1; G5E9S1; O43177; O95066;
Q5HYG0; Q6ZN21; Q8N102;
01-FEB-1995, integrated into UniProtKB/Swiss-Prot.
20-APR-2010, sequence version 4.
27-SEP-2017, entry version 198.
RecName: Full=Eukaryotic translation initiation factor 4 gamma 1;
Short=eIF-4-gamma 1;
Short=eIF-4G 1;
Short=eIF-4G1;
AltName: Full=p220;
Name=EIF4G1; Synonyms=EIF4F, EIF4G, EIF4GI;
Homo sapiens (Human).
Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
Catarrhini; Hominidae; Homo.
NCBI_TaxID=9606;
[1]
NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 7), AND VARIANT VAL-432.
TISSUE=Brain;
PubMed=1429670;
Yan R., Rychlik W., Etchison D., Rhoads R.E.;
"Amino acid sequence of the human protein synthesis initiation factor
eIF-4 gamma.";
J. Biol. Chem. 267:23226-23231(1992).
[2]
NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM B), AND INTERACTION WITH PABPC1.
PubMed=9857202; DOI=10.1093/emboj/17.24.7480;
Imataka H., Gradi A., Sonenberg N.;
"A newly identified N-terminal amino acid sequence of human eIF4G
binds poly(A)-binding protein and functions in poly(A)-dependent
translation.";
EMBO J. 17:7480-7489(1998).
[3]
NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM C).
PubMed=9418880; DOI=10.1128/MCB.18.1.334;
Gradi A., Imataka H., Svitkin Y.V., Rom E., Raught B., Morino S.,
Sonenberg N.;
"A novel functional human eukaryotic translation initiation factor
4G.";
Mol. Cell. Biol. 18:334-342(1998).
[4]
NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 8), VARIANTS ALA-161 AND VAL-432,
AND ALTERNATIVE INITIATION.
PubMed=12052860; DOI=10.1128/MCB.22.13.4499-4511.2002;
Byrd M.P., Zamora M., Lloyd R.E.;
"Generation of multiple isoforms of eukaryotic translation initiation
factor 4GI by use of alternate translation initiation codons.";
Mol. Cell. Biol. 22:4499-4511(2002).
[5]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM A).
PubMed=14702039; DOI=10.1038/ng1285;
Ota T., Suzuki Y., Nishikawa T., Otsuki T., Sugiyama T., Irie R.,
Wakamatsu A., Hayashi K., Sato H., Nagai K., Kimura K., Makita H.,
Sekine M., Obayashi M., Nishi T., Shibahara T., Tanaka T., Ishii S.,
Yamamoto J., Saito K., Kawai Y., Isono Y., Nakamura Y., Nagahari K.,
Murakami K., Yasuda T., Iwayanagi T., Wagatsuma M., Shiratori A.,
Sudo H., Hosoiri T., Kaku Y., Kodaira H., Kondo H., Sugawara M.,
Takahashi M., Kanda K., Yokoi T., Furuya T., Kikkawa E., Omura Y.,
Abe K., Kamihara K., Katsuta N., Sato K., Tanikawa M., Yamazaki M.,
Ninomiya K., Ishibashi T., Yamashita H., Murakawa K., Fujimori K.,
Tanai H., Kimata M., Watanabe M., Hiraoka S., Chiba Y., Ishida S.,
Ono Y., Takiguchi S., Watanabe S., Yosida M., Hotuta T., Kusano J.,
Kanehori K., Takahashi-Fujii A., Hara H., Tanase T.-O., Nomura Y.,
Togiya S., Komai F., Hara R., Takeuchi K., Arita M., Imose N.,
Musashino K., Yuuki H., Oshima A., Sasaki N., Aotsuka S.,
Yoshikawa Y., Matsunawa H., Ichihara T., Shiohata N., Sano S.,
Moriya S., Momiyama H., Satoh N., Takami S., Terashima Y., Suzuki O.,
Nakagawa S., Senoh A., Mizoguchi H., Goto Y., Shimizu F., Wakebe H.,
Hishigaki H., Watanabe T., Sugiyama A., Takemoto M., Kawakami B.,
Yamazaki M., Watanabe K., Kumagai A., Itakura S., Fukuzumi Y.,
Fujimori Y., Komiyama M., Tashiro H., Tanigami A., Fujiwara T.,
Ono T., Yamada K., Fujii Y., Ozaki K., Hirao M., Ohmori Y.,
Kawabata A., Hikiji T., Kobatake N., Inagaki H., Ikema Y., Okamoto S.,
Okitani R., Kawakami T., Noguchi S., Itoh T., Shigeta K., Senba T.,
Matsumura K., Nakajima Y., Mizuno T., Morinaga M., Sasaki M.,
Togashi T., Oyama M., Hata H., Watanabe M., Komatsu T.,
Mizushima-Sugano J., Satoh T., Shirai Y., Takahashi Y., Nakagawa K.,
Okumura K., Nagase T., Nomura N., Kikuchi H., Masuho Y., Yamashita R.,
Nakai K., Yada T., Nakamura Y., Ohara O., Isogai T., Sugano S.;
"Complete sequencing and characterization of 21,243 full-length human
cDNAs.";
Nat. Genet. 36:40-45(2004).
[6]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM A), AND VARIANT
ALA-161.
TISSUE=Endometrial tumor;
PubMed=17974005; DOI=10.1186/1471-2164-8-399;
Bechtel S., Rosenfelder H., Duda A., Schmidt C.P., Ernst U.,
Wellenreuther R., Mehrle A., Schuster C., Bahr A., Bloecker H.,
Heubner D., Hoerlein A., Michel G., Wedler H., Koehrer K.,
Ottenwaelder B., Poustka A., Wiemann S., Schupp I.;
"The full-ORF clone resource of the German cDNA consortium.";
BMC Genomics 8:399-399(2007).
[7]
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
PubMed=16641997; DOI=10.1038/nature04728;
Muzny D.M., Scherer S.E., Kaul R., Wang J., Yu J., Sudbrak R.,
Buhay C.J., Chen R., Cree A., Ding Y., Dugan-Rocha S., Gill R.,
Gunaratne P., Harris R.A., Hawes A.C., Hernandez J., Hodgson A.V.,
Hume J., Jackson A., Khan Z.M., Kovar-Smith C., Lewis L.R.,
Lozado R.J., Metzker M.L., Milosavljevic A., Miner G.R., Morgan M.B.,
Nazareth L.V., Scott G., Sodergren E., Song X.-Z., Steffen D., Wei S.,
Wheeler D.A., Wright M.W., Worley K.C., Yuan Y., Zhang Z., Adams C.Q.,
Ansari-Lari M.A., Ayele M., Brown M.J., Chen G., Chen Z.,
Clendenning J., Clerc-Blankenburg K.P., Chen R., Chen Z., Davis C.,
Delgado O., Dinh H.H., Dong W., Draper H., Ernst S., Fu G.,
Gonzalez-Garay M.L., Garcia D.K., Gillett W., Gu J., Hao B.,
Haugen E., Havlak P., He X., Hennig S., Hu S., Huang W., Jackson L.R.,
Jacob L.S., Kelly S.H., Kube M., Levy R., Li Z., Liu B., Liu J.,
Liu W., Lu J., Maheshwari M., Nguyen B.-V., Okwuonu G.O., Palmeiri A.,
Pasternak S., Perez L.M., Phelps K.A., Plopper F.J., Qiang B.,
Raymond C., Rodriguez R., Saenphimmachak C., Santibanez J., Shen H.,
Shen Y., Subramanian S., Tabor P.E., Verduzco D., Waldron L., Wang J.,
Wang J., Wang Q., Williams G.A., Wong G.K.-S., Yao Z., Zhang J.,
Zhang X., Zhao G., Zhou J., Zhou Y., Nelson D., Lehrach H.,
Reinhardt R., Naylor S.L., Yang H., Olson M., Weinstock G.,
Gibbs R.A.;
"The DNA sequence, annotation and analysis of human chromosome 3.";
Nature 440:1194-1198(2006).
[8]
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Mural R.J., Istrail S., Sutton G.G., Florea L., Halpern A.L.,
Mobarry C.M., Lippert R., Walenz B., Shatkay H., Dew I., Miller J.R.,
Flanigan M.J., Edwards N.J., Bolanos R., Fasulo D., Halldorsson B.V.,
Hannenhalli S., Turner R., Yooseph S., Lu F., Nusskern D.R.,
Shue B.C., Zheng X.H., Zhong F., Delcher A.L., Huson D.H.,
Kravitz S.A., Mouchard L., Reinert K., Remington K.A., Clark A.G.,
Waterman M.S., Eichler E.E., Adams M.D., Hunkapiller M.W., Myers E.W.,
Venter J.C.;
Submitted (SEP-2005) to the EMBL/GenBank/DDBJ databases.
[9]
NUCLEOTIDE SEQUENCE [MRNA] OF 30-206, NUCLEOTIDE SEQUENCE [GENOMIC
DNA] OF 180-234, VARIANT ALA-161, AND INTERACTION WITH ROTAVIRAL NSP3.
PubMed=9755181; DOI=10.1093/emboj/17.19.5811;
Piron M., Vende P., Cohen J., Poncet D.;
"Rotavirus RNA binding protein NSP3, interacts with eIF-4GI and evicts
the poly(A) binding protein from eIF4F.";
EMBO J. 17:5811-5821(1998).
[10]
NUCLEOTIDE SEQUENCE [MRNA] OF 37-1599 (ISOFORM 8), INTERACTION WITH
EIF4A, VARIANTS ALA-161 AND VAL-432, AND MUTAGENESIS OF LEU-768;
LEU-771; PHE-776; 842-LEU-LEU-843; 851-PHE-GLU-852; LEU-896; ILE-902;
LEU-905; ARG-974; PHE-977; LEU-985 AND TRP-990.
PubMed=9372926; DOI=10.1128/MCB.17.12.6940;
Imataka H., Sonenberg N.;
"Human eukaryotic translation initiation factor 4G (eIF4G) possesses
two separate and independent binding sites for eIF4A.";
Mol. Cell. Biol. 17:6940-6947(1997).
[11]
NUCLEOTIDE SEQUENCE [MRNA] OF 605-721, INTERACTION WITH EIF4E, AND
MUTAGENESIS OF TYR-612 AND 617-LEU-LEU-618.
PubMed=7651417; DOI=10.1128/MCB.15.9.4990;
Mader S., Lee H., Pause A., Sonenberg N.;
"The translation initiation factor eIF-4E binds to a common motif
shared by the translation factor eIF-4 gamma and the translational
repressors 4E-binding proteins.";
Mol. Cell. Biol. 15:4990-4997(1995).
[12]
NUCLEOTIDE SEQUENCE [MRNA] OF 682-912 (ISOFORM 8).
De Gregorio E.;
Submitted (AUG-1997) to the EMBL/GenBank/DDBJ databases.
[13]
CLEAVAGE BY RHINOVIRUS AND COXSACKIEVIRUS PROTEASE.
PubMed=8396129;
Lamphear B.J., Yan R., Yang F., Waters D., Liebig H.-D., Klump H.,
Kuechler E., Skern T., Rhoads R.E.;
"Mapping the cleavage site in protein synthesis initiation factor eIF-
4 gamma of the 2A proteases from human Coxsackievirus and
rhinovirus.";
J. Biol. Chem. 268:19200-19203(1993).
[14]
INTERACTION WITH EIF4E.
TISSUE=Placenta;
PubMed=7935836; DOI=10.1038/371762a0;
Pause A., Belsham G.J., Gingras A.-C., Donze O., Lin T.-A.,
Lawrence J.C. Jr., Sonenberg N.;
"Insulin-dependent stimulation of protein synthesis by phosphorylation
of a regulator of 5'-cap function.";
Nature 371:762-767(1994).
[15]
INTERACTION WITH EIF4E AND EIF4EBP1.
PubMed=8521827;
Haghighat A., Mader S., Pause A., Sonenberg N.;
"Repression of cap-dependent translation by 4E-binding protein 1:
competition with p220 for binding to eukaryotic initiation factor-
4E.";
EMBO J. 14:5701-5709(1995).
[16]
MUTAGENESIS OF GLY-682.
PubMed=8961935; DOI=10.1021/bi961864t;
Lamphear B.J., Rhoads R.E.;
"A single amino acid change in protein synthesis initiation factor 4G
renders cap-dependent translation resistant to picornaviral 2A
proteases.";
Biochemistry 35:15726-15733(1996).
[17]
CLEAVAGE BY POLIOVIRUS.
PubMed=9755863; DOI=10.1016/S0014-5793(98)01027-8;
Ventoso I., MacMillan S.E., Hershey J.W., Carrasco L.;
"Poliovirus 2A proteinase cleaves directly the eIF-4G subunit of eIF-
4F complex.";
FEBS Lett. 435:79-83(1998).
[18]
REVIEW.
PubMed=10872469; DOI=10.1146/annurev.biochem.68.1.913;
Gingras A.-C., Raught B., Sonenberg N.;
"eIF4 initiation factors: effectors of mRNA recruitment to ribosomes
and regulators of translation.";
Annu. Rev. Biochem. 68:913-963(1999).
[19]
INTERACTION WITH MKNK1.
PubMed=9878069; DOI=10.1093/emboj/18.1.270;
Pyronnet S., Imataka H., Gingras A.-C., Fukunaga R., Hunter T.,
Sonenberg N.;
"Human eukaryotic translation initiation factor 4G (eIF4G) recruits
mnk1 to phosphorylate eIF4E.";
EMBO J. 18:270-279(1999).
[20]
INTERACTION WITH PABPC1, AND MUTAGENESIS OF 174-LYS--LYS-178 AND
184-ASP--GLN-197.
PubMed=10996799; DOI=10.1016/S0960-9822(00)00701-6;
Wakiyama M., Imataka H., Sonenberg N.;
"Interaction of eIF4G with poly(A)-binding protein stimulates
translation and is critical for Xenopus oocyte maturation.";
Curr. Biol. 10:1147-1150(2000).
[21]
INTERACTION WITH PABPC1.
PubMed=10970864; DOI=10.1093/emboj/19.17.4723;
Gray N.K., Coller J.M., Dickson K.S., Wickens M.;
"Multiple portions of poly(A)-binding protein stimulate translation in
vivo.";
EMBO J. 19:4723-4733(2000).
[22]
CLEAVAGE BY FMDV AND HRV-2.
PubMed=11034318; DOI=10.1016/S0014-5793(00)01928-1;
Glaser W., Skern T.;
"Extremely efficient cleavage of eIF4G by picornaviral proteinases L
and 2A in vitro.";
FEBS Lett. 480:151-155(2000).
[23]
INTERACTION WITH MKNK2.
PubMed=11154262; DOI=10.1128/MCB.21.3.743-754.2001;
Scheper G.C., Morrice N.A., Kleijn M., Proud C.G.;
"The mitogen-activated protein kinase signal-integrating kinase Mnk2
is a eukaryotic initiation factor 4E kinase with high levels of basal
activity in mammalian cells.";
Mol. Cell. Biol. 21:743-754(2001).
[24]
INTERACTION WITH HADV5 100K PROTEIN.
PubMed=15314025; DOI=10.1101/gad.1212504;
Xi Q., Cuesta R., Schneider R.J.;
"Tethering of eIF4G to adenoviral mRNAs by viral 100k protein drives
ribosome shunting.";
Genes Dev. 18:1997-2009(2004).
[25]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-1231, AND IDENTIFICATION
BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
TISSUE=Cervix carcinoma;
PubMed=17081983; DOI=10.1016/j.cell.2006.09.026;
Olsen J.V., Blagoev B., Gnad F., Macek B., Kumar C., Mortensen P.,
Mann M.;
"Global, in vivo, and site-specific phosphorylation dynamics in
signaling networks.";
Cell 127:635-648(2006).
[26]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-1231, AND IDENTIFICATION
BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
TISSUE=Cervix carcinoma;
PubMed=16964243; DOI=10.1038/nbt1240;
Beausoleil S.A., Villen J., Gerber S.A., Rush J., Gygi S.P.;
"A probability-based approach for high-throughput protein
phosphorylation analysis and site localization.";
Nat. Biotechnol. 24:1285-1292(2006).
[27]
INTERACTION WITH CIRBP.
PubMed=16513844; DOI=10.1093/nar/gkj519;
Yang R., Weber D.J., Carrier F.;
"Post-transcriptional regulation of thioredoxin by the stress
inducible heterogeneous ribonucleoprotein A18.";
Nucleic Acids Res. 34:1224-1236(2006).
[28]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-1092, AND IDENTIFICATION
BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
TISSUE=Cervix carcinoma;
PubMed=17924679; DOI=10.1021/pr070152u;
Yu L.R., Zhu Z., Chan K.C., Issaq H.J., Dimitrov D.S., Veenstra T.D.;
"Improved titanium dioxide enrichment of phosphopeptides from HeLa
cells and high confident phosphopeptide identification by cross-
validation of MS/MS and MS/MS/MS spectra.";
J. Proteome Res. 6:4150-4162(2007).
[29]
INTERACTION WITH RBM4.
PubMed=17284590; DOI=10.1073/pnas.0611015104;
Lin J.C., Hsu M., Tarn W.Y.;
"Cell stress modulates the function of splicing regulatory protein
RBM4 in translation control.";
Proc. Natl. Acad. Sci. U.S.A. 104:2235-2240(2007).
[30]
IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
TISSUE=Platelet;
PubMed=18088087; DOI=10.1021/pr0704130;
Zahedi R.P., Lewandrowski U., Wiesner J., Wortelkamp S., Moebius J.,
Schuetz C., Walter U., Gambaryan S., Sickmann A.;
"Phosphoproteome of resting human platelets.";
J. Proteome Res. 7:526-534(2008).
[31]
INTERACTION WITH ROTAVIRUS A NSP3.
PubMed=18799579; DOI=10.1128/JVI.00872-08;
Harb M., Becker M.M., Vitour D., Baron C.H., Vende P., Brown S.C.,
Bolte S., Arold S.T., Poncet D.;
"Nuclear localization of cytoplasmic poly(A)-binding protein upon
rotavirus infection involves the interaction of NSP3 with eIF4G and
RoXaN.";
J. Virol. 82:11283-11293(2008).
[32]
INTERACTION WITH MIF4GD.
PubMed=18025107; DOI=10.1128/MCB.01500-07;
Cakmakci N.G., Lerner R.S., Wagner E.J., Zheng L., Marzluff W.F.;
"SLIP1, a factor required for activation of histone mRNA translation
by the stem-loop binding protein.";
Mol. Cell. Biol. 28:1182-1194(2008).
[33]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-207; THR-223; THR-647;
SER-1092 AND SER-1209, AND IDENTIFICATION BY MASS SPECTROMETRY [LARGE
SCALE ANALYSIS].
TISSUE=Cervix carcinoma;
PubMed=18669648; DOI=10.1073/pnas.0805139105;
Dephoure N., Zhou C., Villen J., Beausoleil S.A., Bakalarski C.E.,
Elledge S.J., Gygi S.P.;
"A quantitative atlas of mitotic phosphorylation.";
Proc. Natl. Acad. Sci. U.S.A. 105:10762-10767(2008).
[34]
IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
PubMed=19369195; DOI=10.1074/mcp.M800588-MCP200;
Oppermann F.S., Gnad F., Olsen J.V., Hornberger R., Greff Z., Keri G.,
Mann M., Daub H.;
"Large-scale proteomics analysis of the human kinome.";
Mol. Cell. Proteomics 8:1751-1764(2009).
[35]
IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
TISSUE=Leukemic T-cell;
PubMed=19690332; DOI=10.1126/scisignal.2000007;
Mayya V., Lundgren D.H., Hwang S.-I., Rezaul K., Wu L., Eng J.K.,
Rodionov V., Han D.K.;
"Quantitative phosphoproteomic analysis of T cell receptor signaling
reveals system-wide modulation of protein-protein interactions.";
Sci. Signal. 2:RA46-RA46(2009).
[36]
ACETYLATION [LARGE SCALE ANALYSIS] AT LYS-1095, AND IDENTIFICATION BY
MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
PubMed=19608861; DOI=10.1126/science.1175371;
Choudhary C., Kumar C., Gnad F., Nielsen M.L., Rehman M.,
Walther T.C., Olsen J.V., Mann M.;
"Lysine acetylation targets protein complexes and co-regulates major
cellular functions.";
Science 325:834-840(2009).
[37]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-1028; SER-1092;
SER-1185; SER-1187; SER-1209; THR-1211; SER-1231 AND SER-1596, AND
IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
TISSUE=Cervix carcinoma;
PubMed=20068231; DOI=10.1126/scisignal.2000475;
Olsen J.V., Vermeulen M., Santamaria A., Kumar C., Miller M.L.,
Jensen L.J., Gnad F., Cox J., Jensen T.S., Nigg E.A., Brunak S.,
Mann M.;
"Quantitative phosphoproteomics reveals widespread full
phosphorylation site occupancy during mitosis.";
Sci. Signal. 3:RA3-RA3(2010).
[38]
IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
PubMed=21269460; DOI=10.1186/1752-0509-5-17;
Burkard T.R., Planyavsky M., Kaupe I., Breitwieser F.P.,
Buerckstuemmer T., Bennett K.L., Superti-Furga G., Colinge J.;
"Initial characterization of the human central proteome.";
BMC Syst. Biol. 5:17-17(2011).
[39]
PHOSPHORYLATION AT SER-1185.
PubMed=21576361; DOI=10.1128/MCB.05589-11;
Dobrikov M., Dobrikova E., Shveygert M., Gromeier M.;
"Phosphorylation of eukaryotic translation initiation factor 4G1
(eIF4G1) by protein kinase C{alpha} regulates eIF4G1 binding to
Mnk1.";
Mol. Cell. Biol. 31:2947-2959(2011).
[40]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-1028; SER-1092;
SER-1145; SER-1147; SER-1185; SER-1187; SER-1209; THR-1211; SER-1231
AND SER-1596, AND IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE
ANALYSIS].
PubMed=21406692; DOI=10.1126/scisignal.2001570;
Rigbolt K.T., Prokhorova T.A., Akimov V., Henningsen J.,
Johansen P.T., Kratchmarova I., Kassem M., Mann M., Olsen J.V.,
Blagoev B.;
"System-wide temporal characterization of the proteome and
phosphoproteome of human embryonic stem cell differentiation.";
Sci. Signal. 4:RS3-RS3(2011).
[41]
ACETYLATION [LARGE SCALE ANALYSIS] AT MET-2 (ISOFORM C), CLEAVAGE OF
INITIATOR METHIONINE [LARGE SCALE ANALYSIS] (ISOFORM C), AND
IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
PubMed=22814378; DOI=10.1073/pnas.1210303109;
Van Damme P., Lasa M., Polevoda B., Gazquez C., Elosegui-Artola A.,
Kim D.S., De Juan-Pardo E., Demeyer K., Hole K., Larrea E.,
Timmerman E., Prieto J., Arnesen T., Sherman F., Gevaert K.,
Aldabe R.;
"N-terminal acetylome analyses and functional insights of the N-
terminal acetyltransferase NatB.";
Proc. Natl. Acad. Sci. U.S.A. 109:12449-12454(2012).
[42]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-207; THR-647; SER-1028;
SER-1077; SER-1092; SER-1145; SER-1147; SER-1185; SER-1187; SER-1194;
SER-1209; SER-1231; SER-1238 AND SER-1596, PHOSPHORYLATION [LARGE
SCALE ANALYSIS] AT SER-509 (ISOFORM 7), PHOSPHORYLATION [LARGE SCALE
ANALYSIS] AT SER-705 (ISOFORM 8), AND IDENTIFICATION BY MASS
SPECTROMETRY [LARGE SCALE ANALYSIS].
TISSUE=Cervix carcinoma, and Erythroleukemia;
PubMed=23186163; DOI=10.1021/pr300630k;
Zhou H., Di Palma S., Preisinger C., Peng M., Polat A.N., Heck A.J.,
Mohammed S.;
"Toward a comprehensive characterization of a human cancer cell
phosphoproteome.";
J. Proteome Res. 12:260-271(2013).
[43]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-314, AND IDENTIFICATION
BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
TISSUE=Liver;
PubMed=24275569; DOI=10.1016/j.jprot.2013.11.014;
Bian Y., Song C., Cheng K., Dong M., Wang F., Huang J., Sun D.,
Wang L., Ye M., Zou H.;
"An enzyme assisted RP-RPLC approach for in-depth analysis of human
liver phosphoproteome.";
J. Proteomics 96:253-262(2014).
[44]
METHYLATION [LARGE SCALE ANALYSIS] AT ARG-73; ARG-110; ARG-685;
ARG-694; ARG-1032 AND ARG-1042, METHYLATION [LARGE SCALE ANALYSIS] AT
ARG-489 AND ARG-498 (ISOFORM 7), METHYLATION [LARGE SCALE ANALYSIS] AT
ARG-685 AND ARG-694 (ISOFORM 8), AND IDENTIFICATION BY MASS
SPECTROMETRY [LARGE SCALE ANALYSIS].
TISSUE=Colon carcinoma;
PubMed=24129315; DOI=10.1074/mcp.O113.027870;
Guo A., Gu H., Zhou J., Mulhern D., Wang Y., Lee K.A., Yang V.,
Aguiar M., Kornhauser J., Jia X., Ren J., Beausoleil S.A., Silva J.C.,
Vemulapalli V., Bedford M.T., Comb M.J.;
"Immunoaffinity enrichment and mass spectrometry analysis of protein
methylation.";
Mol. Cell. Proteomics 13:372-387(2014).
[45]
INTERACTION WITH HNRPD, AND RNA-BINDING.
PubMed=24423872; DOI=10.1093/nar/gkt1379;
Lee K.H., Kim S.H., Kim H.J., Kim W., Lee H.R., Jung Y., Choi J.H.,
Hong K.Y., Jang S.K., Kim K.T.;
"AUF1 contributes to Cryptochrome1 mRNA degradation and rhythmic
translation.";
Nucleic Acids Res. 42:3590-3606(2014).
[46]
X-RAY CRYSTALLOGRAPHY (2.38 ANGSTROMS) OF 172-199 IN COMPLEX WITH
ROTAVIRAL NSP3, INTERACTION WITH PABPC1, AND MUTAGENESIS OF ILE-180;
ILE-182; ILE-192 AND ILE-196.
PubMed=12086624; DOI=10.1016/S1097-2765(02)00555-5;
Groft C.M., Burley S.K.;
"Recognition of eIF4G by rotavirus NSP3 reveals a basis for mRNA
circularization.";
Mol. Cell 9:1273-1283(2002).
[47]
X-RAY CRYSTALLOGRAPHY (2.24 ANGSTROMS) OF 1234-1571.
PubMed=16698552; DOI=10.1016/j.str.2006.03.012;
Bellsolell L., Cho-Park P.F., Poulin F., Sonenberg N., Burley S.K.;
"Two structurally atypical HEAT domains in the C-terminal portion of
human eIF4G support binding to eIF4A and Mnk1.";
Structure 14:913-923(2006).
[48]
VARIANT [LARGE SCALE ANALYSIS] LEU-696.
PubMed=16959974; DOI=10.1126/science.1133427;
Sjoeblom T., Jones S., Wood L.D., Parsons D.W., Lin J., Barber T.D.,
Mandelker D., Leary R.J., Ptak J., Silliman N., Szabo S.,
Buckhaults P., Farrell C., Meeh P., Markowitz S.D., Willis J.,
Dawson D., Willson J.K.V., Gazdar A.F., Hartigan J., Wu L., Liu C.,
Parmigiani G., Park B.H., Bachman K.E., Papadopoulos N.,
Vogelstein B., Kinzler K.W., Velculescu V.E.;
"The consensus coding sequences of human breast and colorectal
cancers.";
Science 314:268-274(2006).
[49]
VARIANT [LARGE SCALE ANALYSIS] VAL-432, AND IDENTIFICATION BY MASS
SPECTROMETRY [LARGE SCALE ANALYSIS].
PubMed=19413330; DOI=10.1021/ac9004309;
Gauci S., Helbig A.O., Slijper M., Krijgsveld J., Heck A.J.,
Mohammed S.;
"Lys-N and trypsin cover complementary parts of the phosphoproteome in
a refined SCX-based approach.";
Anal. Chem. 81:4493-4501(2009).
[50]
VARIANTS PARK18 VAL-502 AND HIS-1205, AND VARIANTS SER-71; ALA-161;
CYS-311; VAL-432; 466-GLY--ALA-468 DEL; CYS-686; VAL-806; SER-829;
ARG-1164; TRP-1197; ALA-1229; PRO-1233 AND SER-1257.
PubMed=21907011; DOI=10.1016/j.ajhg.2011.08.009;
Chartier-Harlin M.C., Dachsel J.C., Vilarino-Guell C., Lincoln S.J.,
Lepretre F., Hulihan M.M., Kachergus J., Milnerwood A.J., Tapia L.,
Song M.S., Le Rhun E., Mutez E., Larvor L., Duflot A.,
Vanbesien-Mailliot C., Kreisler A., Ross O.A., Nishioka K.,
Soto-Ortolaza A.I., Cobb S.A., Melrose H.L., Behrouz B., Keeling B.H.,
Bacon J.A., Hentati E., Williams L., Yanagiya A., Sonenberg N.,
Lockhart P.J., Zubair A.C., Uitti R.J., Aasly J.O., Krygowska-Wajs A.,
Opala G., Wszolek Z.K., Frigerio R., Maraganore D.M., Gosal D.,
Lynch T., Hutchinson M., Bentivoglio A.R., Valente E.M., Nichols W.C.,
Pankratz N., Foroud T., Gibson R.A., Hentati F., Dickson D.W.,
Destee A., Farrer M.J.;
"Translation initiator EIF4G1 mutations in familial Parkinson
disease.";
Am. J. Hum. Genet. 89:398-406(2011).
-!- FUNCTION: Component of the protein complex eIF4F, which is
involved in the recognition of the mRNA cap, ATP-dependent
unwinding of 5'-terminal secondary structure and recruitment of
mRNA to the ribosome.
-!- SUBUNIT: eIF4F is a multi-subunit complex, the composition of
which varies with external and internal environmental conditions.
It is composed of at least EIF4A, EIF4E (cap-binding) and
EIF4G1/EIF4G3. Interacts with eIF3, mutually exclusive with EIF4A1
or EIFA2, EIF4E and through its N-terminus with PAPBC1. Interacts
through its C-terminus with the serine/threonine kinases MKNK1,
and with MKNK2. Appears to act as a scaffold protein, holding
these enzymes in place to phosphorylate EIF4E. Non-phosphorylated
EIF4EBP1 competes with EIF4G1/EIF4G3 to interact with EIF4E;
insulin stimulated MAP-kinase (MAPK1 and MAPK3) phosphorylation of
EIF4EBP1 causes dissociation of the complex allowing EIF4G1/EIF4G3
to bind and consequent initiation of translation. EIF4G1/EIF4G3
interacts with PABPC1 to bring about circularization of the mRNA.
Rapamycin can attenuate insulin stimulation mediated by FKBPs.
Interacts with EIF4E3. Interacts with CIRBP and MIF4GD. Interacts
with rotavirus A NSP3; in this interaction, NSP3 takes the place
of PABPC1 thereby inducing shutoff of host protein synthesis.
Interacts with RBM4. Interacts with HNRNPD/AUF1; the interaction
requires RNA. Interacts with human adenovirus 5 100K protein; this
interaction promotes translational shunt in presence of polysomes
containing viral tripartite leader mRNAs (PubMed:15314025).
{ECO:0000269|PubMed:10970864, ECO:0000269|PubMed:10996799,
ECO:0000269|PubMed:11154262, ECO:0000269|PubMed:12086624,
ECO:0000269|PubMed:15314025, ECO:0000269|PubMed:16513844,
ECO:0000269|PubMed:17284590, ECO:0000269|PubMed:18025107,
ECO:0000269|PubMed:18799579, ECO:0000269|PubMed:24423872,
ECO:0000269|PubMed:7651417, ECO:0000269|PubMed:7935836,
ECO:0000269|PubMed:8521827, ECO:0000269|PubMed:9372926,
ECO:0000269|PubMed:9755181, ECO:0000269|PubMed:9857202,
ECO:0000269|PubMed:9878069}.
-!- INTERACTION:
Q2TAC2-2:CCDC57; NbExp=4; IntAct=EBI-12012124, EBI-10961624;
O00571:DDX3X; NbExp=3; IntAct=EBI-73711, EBI-353779;
O75822:EIF3J; NbExp=2; IntAct=EBI-73711, EBI-366647;
P60842:EIF4A1; NbExp=11; IntAct=EBI-73711, EBI-73449;
Q14240:EIF4A2; NbExp=4; IntAct=EBI-73711, EBI-73473;
P06730:EIF4E; NbExp=2; IntAct=EBI-73711, EBI-73440;
Q14103-4:HNRNPD; NbExp=3; IntAct=EBI-73711, EBI-432545;
Q9BUB5:MKNK1; NbExp=2; IntAct=EBI-73711, EBI-73837;
P11940:PABPC1; NbExp=4; IntAct=EBI-73711, EBI-81531;
Q9J0X9:UL54 (xeno); NbExp=3; IntAct=EBI-73711, EBI-7967856;
Q9UGR2:ZC3H7B; NbExp=3; IntAct=EBI-73711, EBI-948845;
-!- ALTERNATIVE PRODUCTS:
Event=Alternative splicing, Alternative initiation; Named isoforms=8;
Name=A;
IsoId=Q04637-1; Sequence=Displayed;
Name=B;
IsoId=Q04637-3; Sequence=VSP_018720;
Note=Produced by alternative initiation at Met-41 of isoform A.;
Name=C;
IsoId=Q04637-4; Sequence=VSP_018721;
Note=Produced by alternative initiation at Met-88 of isoform A.
Initiator Met-1 is removed. Contains a N-acetylmethionine at
position 2. {ECO:0000244|PubMed:22814378};
Name=D;
IsoId=Q04637-5; Sequence=VSP_018722;
Note=Produced by alternative initiation at Met-165 of isoform
A.;
Name=E;
IsoId=Q04637-6; Sequence=VSP_018723;
Note=Produced by alternative initiation at Met-197 of isoform
A.;
Name=7;
IsoId=Q04637-7; Sequence=VSP_018723, VSP_047397;
Note=Produced by alternative splicing. Contains a
omega-N-methylarginine at position 489. Contains a
omega-N-methylarginine at position 498. Contains a phosphoserine
at position 509. {ECO:0000244|PubMed:23186163,
ECO:0000244|PubMed:24129315};
Name=8;
IsoId=Q04637-8; Sequence=VSP_047397;
Note=Produced by alternative splicing. Contains a
omega-N-methylarginine at position 685. Contains a
omega-N-methylarginine at position 694. Contains a phosphoserine
at position 705. {ECO:0000244|PubMed:23186163,
ECO:0000244|PubMed:24129315};
Name=9;
IsoId=Q04637-9; Sequence=VSP_047396;
Note=Produced by alternative splicing. Gene prediction based on
EST data.;
-!- PTM: Phosphorylated at multiple sites in vivo. Phosphorylation at
Ser-1185 by PRKCA induces binding to MKNK1.
{ECO:0000269|PubMed:21576361}.
-!- PTM: Following infection by certain enteroviruses, rhinoviruses
and aphthoviruses, EIF4G1 is cleaved by the viral protease 2A, or
the leader protease in the case of aphthoviruses. This shuts down
the capped cellular mRNA transcription.
{ECO:0000269|PubMed:11034318, ECO:0000269|PubMed:8396129,
ECO:0000269|PubMed:9755863}.
-!- DISEASE: Parkinson disease 18 (PARK18) [MIM:614251]: An autosomal
dominant, late-onset form of Parkinson disease. Parkinson disease
is a complex neurodegenerative disorder characterized by
bradykinesia, resting tremor, muscular rigidity and postural
instability, as well as by a clinically significant response to
treatment with levodopa. The pathology involves the loss of
dopaminergic neurons in the substantia nigra and the presence of
Lewy bodies (intraneuronal accumulations of aggregated proteins),
in surviving neurons in various areas of the brain.
{ECO:0000269|PubMed:21907011}. Note=The disease is caused by
mutations affecting the gene represented in this entry.
-!- SIMILARITY: Belongs to the eukaryotic initiation factor 4G family.
{ECO:0000305}.
-!- SEQUENCE CAUTION:
Sequence=AAC78444.1; Type=Erroneous initiation; Note=Translation N-terminally extended.; Evidence={ECO:0000305};
Sequence=AAC82471.1; Type=Erroneous initiation; Note=Translation N-terminally extended.; Evidence={ECO:0000305};
Sequence=BAA02185.1; Type=Frameshift; Positions=Several; Evidence={ECO:0000305};
Sequence=BAD18554.1; Type=Miscellaneous discrepancy; Note=Aberrant splicing.; Evidence={ECO:0000305};
-----------------------------------------------------------------------
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EMBL; D12686; BAA02185.1; ALT_FRAME; mRNA.
EMBL; AY082886; AAL92872.1; -; mRNA.
EMBL; AF281070; AAM69365.1; -; mRNA.
EMBL; AK131407; BAD18554.1; ALT_SEQ; mRNA.
EMBL; BX647812; CAI46013.1; -; mRNA.
EMBL; AC078797; -; NOT_ANNOTATED_CDS; Genomic_DNA.
EMBL; CH471052; EAW78257.1; -; Genomic_DNA.
EMBL; CH471052; EAW78259.1; -; Genomic_DNA.
EMBL; CH471052; EAW78262.1; -; Genomic_DNA.
EMBL; CH471052; EAW78263.1; -; Genomic_DNA.
EMBL; CH471052; EAW78264.1; -; Genomic_DNA.
EMBL; CH471052; EAW78265.1; -; Genomic_DNA.
EMBL; CH471052; EAW78266.1; -; Genomic_DNA.
EMBL; CH471052; EAW78267.1; -; Genomic_DNA.
EMBL; AF002816; AAC78443.1; -; mRNA.
EMBL; AF004836; AAC78444.1; ALT_INIT; Genomic_DNA.
EMBL; AF104913; AAC82471.1; ALT_INIT; mRNA.
EMBL; AJ001046; CAA04500.1; -; mRNA.
CCDS; CCDS3259.1; -. [Q04637-1]
CCDS; CCDS3260.1; -. [Q04637-4]
CCDS; CCDS3261.1; -. [Q04637-5]
CCDS; CCDS46970.2; -. [Q04637-7]
CCDS; CCDS54687.1; -. [Q04637-9]
CCDS; CCDS54688.1; -. [Q04637-8]
CCDS; CCDS77866.1; -. [Q04637-3]
PIR; A44453; A44453.
RefSeq; NP_004944.3; NM_004953.4. [Q04637-7]
RefSeq; NP_886553.3; NM_182917.4.
RefSeq; NP_937884.1; NM_198241.2.
RefSeq; NP_937885.1; NM_198242.2. [Q04637-5]
UniGene; Hs.433750; -.
PDB; 1LJ2; X-ray; 2.38 A; C/D=172-199.
PDB; 1UG3; X-ray; 2.24 A; A/B=1233-1571.
PDB; 2W97; X-ray; 2.29 A; E/F=609-622.
PDB; 4AZA; X-ray; 2.16 A; B/D=609-620.
PDB; 4F02; X-ray; 2.00 A; C/F=178-203.
PDB; 5EHC; X-ray; 2.40 A; B=609-622.
PDB; 5EI3; X-ray; 1.71 A; B=609-622.
PDB; 5EIR; X-ray; 2.69 A; B=609-622.
PDB; 5T46; X-ray; 1.53 A; B/D=592-653.
PDBsum; 1LJ2; -.
PDBsum; 1UG3; -.
PDBsum; 2W97; -.
PDBsum; 4AZA; -.
PDBsum; 4F02; -.
PDBsum; 5EHC; -.
PDBsum; 5EI3; -.
PDBsum; 5EIR; -.
PDBsum; 5T46; -.
ProteinModelPortal; Q04637; -.
SMR; Q04637; -.
BioGrid; 108296; 99.
CORUM; Q04637; -.
DIP; DIP-1161N; -.
ELM; Q04637; -.
IntAct; Q04637; 72.
MINT; MINT-135718; -.
STRING; 9606.ENSP00000338020; -.
BindingDB; Q04637; -.
iPTMnet; Q04637; -.
PhosphoSitePlus; Q04637; -.
SwissPalm; Q04637; -.
BioMuta; EIF4G1; -.
DMDM; 294862538; -.
EPD; Q04637; -.
MaxQB; Q04637; -.
PaxDb; Q04637; -.
PeptideAtlas; Q04637; -.
PRIDE; Q04637; -.
DNASU; 1981; -.
Ensembl; ENST00000342981; ENSP00000343450; ENSG00000114867. [Q04637-8]
Ensembl; ENST00000346169; ENSP00000316879; ENSG00000114867. [Q04637-1]
Ensembl; ENST00000350481; ENSP00000317600; ENSG00000114867. [Q04637-5]
Ensembl; ENST00000352767; ENSP00000338020; ENSG00000114867. [Q04637-9]
Ensembl; ENST00000382330; ENSP00000371767; ENSG00000114867. [Q04637-9]
Ensembl; ENST00000392537; ENSP00000376320; ENSG00000114867. [Q04637-4]
Ensembl; ENST00000414031; ENSP00000391935; ENSG00000114867. [Q04637-3]
Ensembl; ENST00000424196; ENSP00000416255; ENSG00000114867. [Q04637-9]
Ensembl; ENST00000434061; ENSP00000411826; ENSG00000114867. [Q04637-7]
Ensembl; ENST00000435046; ENSP00000404754; ENSG00000114867. [Q04637-6]
GeneID; 1981; -.
KEGG; hsa:1981; -.
UCSC; uc003fnp.4; human. [Q04637-1]
CTD; 1981; -.
DisGeNET; 1981; -.
EuPathDB; HostDB:ENSG00000114867.19; -.
GeneCards; EIF4G1; -.
HGNC; HGNC:3296; EIF4G1.
HPA; CAB014774; -.
HPA; HPA028487; -.
HPA; HPA043866; -.
MalaCards; EIF4G1; -.
MIM; 600495; gene.
MIM; 614251; phenotype.
neXtProt; NX_Q04637; -.
OpenTargets; ENSG00000114867; -.
Orphanet; 2828; Young adult-onset Parkinsonism.
PharmGKB; PA27722; -.
eggNOG; KOG0401; Eukaryota.
eggNOG; ENOG410XS4P; LUCA.
GeneTree; ENSGT00530000063038; -.
HOGENOM; HOG000231658; -.
HOVERGEN; HBG052083; -.
InParanoid; Q04637; -.
KO; K03260; -.
OMA; AIAREHM; -.
OrthoDB; EOG091G03ZW; -.
PhylomeDB; Q04637; -.
TreeFam; TF101527; -.
Reactome; R-HSA-1169408; ISG15 antiviral mechanism.
Reactome; R-HSA-156827; L13a-mediated translational silencing of Ceruloplasmin expression.
Reactome; R-HSA-166208; mTORC1-mediated signalling.
Reactome; R-HSA-429947; Deadenylation of mRNA.
Reactome; R-HSA-450408; AUF1 (hnRNP D0) binds and destabilizes mRNA.
Reactome; R-HSA-72649; Translation initiation complex formation.
Reactome; R-HSA-72662; Activation of the mRNA upon binding of the cap-binding complex and eIFs, and subsequent binding to 43S.
Reactome; R-HSA-72702; Ribosomal scanning and start codon recognition.
Reactome; R-HSA-72706; GTP hydrolysis and joining of the 60S ribosomal subunit.
Reactome; R-HSA-975956; Nonsense Mediated Decay (NMD) independent of the Exon Junction Complex (EJC).
Reactome; R-HSA-975957; Nonsense Mediated Decay (NMD) enhanced by the Exon Junction Complex (EJC).
SIGNOR; Q04637; -.
ChiTaRS; EIF4G1; human.
EvolutionaryTrace; Q04637; -.
GeneWiki; Eukaryotic_translation_initiation_factor_4_gamma; -.
GenomeRNAi; 1981; -.
PMAP-CutDB; Q04637; -.
PRO; PR:Q04637; -.
Proteomes; UP000005640; Chromosome 3.
Bgee; ENSG00000114867; -.
CleanEx; HS_EIF4G1; -.
ExpressionAtlas; Q04637; baseline and differential.
Genevisible; Q04637; HS.
GO; GO:0005737; C:cytoplasm; IDA:AgBase.
GO; GO:0005829; C:cytosol; TAS:Reactome.
GO; GO:0016281; C:eukaryotic translation initiation factor 4F complex; IDA:ParkinsonsUK-UCL.
GO; GO:0016020; C:membrane; IDA:UniProtKB.
GO; GO:0005634; C:nucleus; IMP:ParkinsonsUK-UCL.
GO; GO:0005844; C:polysome; IMP:ParkinsonsUK-UCL.
GO; GO:0005524; F:ATP binding; IDA:ParkinsonsUK-UCL.
GO; GO:0045296; F:cadherin binding; IDA:BHF-UCL.
GO; GO:0008190; F:eukaryotic initiation factor 4E binding; IDA:AgBase.
GO; GO:0003729; F:mRNA binding; IDA:ParkinsonsUK-UCL.
GO; GO:0032947; F:protein complex scaffold activity; TAS:ParkinsonsUK-UCL.
GO; GO:0003723; F:RNA binding; IDA:UniProtKB.
GO; GO:0008135; F:translation factor activity, RNA binding; IMP:ParkinsonsUK-UCL.
GO; GO:0003743; F:translation initiation factor activity; TAS:UniProtKB.
GO; GO:0031369; F:translation initiation factor binding; TAS:ParkinsonsUK-UCL.
GO; GO:0001662; P:behavioral fear response; IEA:Ensembl.
GO; GO:0002191; P:cap-dependent translational initiation; TAS:ParkinsonsUK-UCL.
GO; GO:0034645; P:cellular macromolecule biosynthetic process; IGI:ParkinsonsUK-UCL.
GO; GO:0032502; P:developmental process; TAS:ParkinsonsUK-UCL.
GO; GO:0007005; P:mitochondrion organization; IMP:ParkinsonsUK-UCL.
GO; GO:0010507; P:negative regulation of autophagy; IMP:ParkinsonsUK-UCL.
GO; GO:1901215; P:negative regulation of neuron death; TAS:ParkinsonsUK-UCL.
GO; GO:0010801; P:negative regulation of peptidyl-threonine phosphorylation; IMP:ParkinsonsUK-UCL.
GO; GO:0000184; P:nuclear-transcribed mRNA catabolic process, nonsense-mediated decay; TAS:Reactome.
GO; GO:0000289; P:nuclear-transcribed mRNA poly(A) tail shortening; TAS:Reactome.
GO; GO:0030307; P:positive regulation of cell growth; IMP:ParkinsonsUK-UCL.
GO; GO:0008284; P:positive regulation of cell proliferation; IMP:ParkinsonsUK-UCL.
GO; GO:0032270; P:positive regulation of cellular protein metabolic process; IMP:ParkinsonsUK-UCL.
GO; GO:2000507; P:positive regulation of energy homeostasis; IMP:ParkinsonsUK-UCL.
GO; GO:1905537; P:positive regulation of eukaryotic translation initiation factor 4F complex assembly; IMP:ParkinsonsUK-UCL.
GO; GO:1900087; P:positive regulation of G1/S transition of mitotic cell cycle; IMP:ParkinsonsUK-UCL.
GO; GO:1905618; P:positive regulation of miRNA mediated inhibition of translation; IDA:ParkinsonsUK-UCL.
GO; GO:1905612; P:positive regulation of mRNA cap binding; IDA:ParkinsonsUK-UCL.
GO; GO:0045666; P:positive regulation of neuron differentiation; IEA:Ensembl.
GO; GO:0033138; P:positive regulation of peptidyl-serine phosphorylation; IMP:ParkinsonsUK-UCL.
GO; GO:0080135; P:regulation of cellular response to stress; TAS:ParkinsonsUK-UCL.
GO; GO:0060964; P:regulation of gene silencing by miRNA; TAS:ParkinsonsUK-UCL.
GO; GO:0043488; P:regulation of mRNA stability; TAS:Reactome.
GO; GO:1905696; P:regulation of polysome binding; IMP:ParkinsonsUK-UCL.
GO; GO:1905606; P:regulation of presynapse assembly; IGI:ParkinsonsUK-UCL.
GO; GO:0006446; P:regulation of translational initiation; IMP:UniProtKB.
GO; GO:0006412; P:translation; IMP:ParkinsonsUK-UCL.
GO; GO:0006413; P:translational initiation; TAS:ParkinsonsUK-UCL.
GO; GO:0016032; P:viral process; IEA:UniProtKB-KW.
InterPro; IPR016024; ARM-type_fold.
InterPro; IPR003891; Initiation_fac_eIF4g_MI.
InterPro; IPR003890; MIF4G-like_typ-3.
InterPro; IPR003307; W2_domain.
Pfam; PF02847; MA3; 1.
Pfam; PF02854; MIF4G; 1.
Pfam; PF02020; W2; 1.
SMART; SM00515; eIF5C; 1.
SMART; SM00544; MA3; 1.
SMART; SM00543; MIF4G; 1.
SUPFAM; SSF48371; SSF48371; 3.
PROSITE; PS51366; MI; 1.
PROSITE; PS51363; W2; 1.
1: Evidence at protein level;
3D-structure; Acetylation; Alternative initiation;
Alternative splicing; Complete proteome; Disease mutation;
Host-virus interaction; Initiation factor; Methylation;
Neurodegeneration; Parkinson disease; Parkinsonism; Phosphoprotein;
Polymorphism; Protein biosynthesis; Reference proteome; RNA-binding;
Translation regulation; Translational shunt.
CHAIN 1 1599 Eukaryotic translation initiation factor
4 gamma 1.
/FTId=PRO_0000007786.
DOMAIN 565 792 MIF4G. {ECO:0000255|PROSITE-
ProRule:PRU00698}.
DOMAIN 1241 1363 MI. {ECO:0000255|PROSITE-
ProRule:PRU00698}.
DOMAIN 1433 1599 W2. {ECO:0000255|PROSITE-
ProRule:PRU00695}.
REGION 172 200 PABPC1-binding.
REGION 607 618 EIF4E-binding.
REGION 682 1085 eIF3/EIF4A-binding.
REGION 1450 1599 EIF4A-binding.
REGION 1585 1599 Necessary but not sufficient for MKNK1-
binding.
COMPBIAS 454 467 Poly-Glu.
COMPBIAS 501 504 Poly-Ala.
SITE 674 675 Cleavage; by foot-and-mouth disease virus
leader protease.
SITE 681 682 Cleavage; by enterovirus/rhinovirus
protease 2A.
MOD_RES 15 15 Phosphoserine.
{ECO:0000250|UniProtKB:Q6NZJ6}.
MOD_RES 73 73 Omega-N-methylarginine.
{ECO:0000244|PubMed:24129315}.
MOD_RES 110 110 Omega-N-methylarginine.
{ECO:0000244|PubMed:24129315}.
MOD_RES 207 207 Phosphothreonine.
{ECO:0000244|PubMed:18669648,
ECO:0000244|PubMed:23186163}.
MOD_RES 223 223 Phosphothreonine.
{ECO:0000244|PubMed:18669648}.
MOD_RES 314 314 Phosphoserine.
{ECO:0000244|PubMed:24275569}.
MOD_RES 602 602 N6-acetyllysine.
{ECO:0000250|UniProtKB:Q6NZJ6}.
MOD_RES 647 647 Phosphothreonine.
{ECO:0000244|PubMed:18669648,
ECO:0000244|PubMed:23186163}.
MOD_RES 685 685 Omega-N-methylarginine.
{ECO:0000244|PubMed:24129315}.
MOD_RES 694 694 Omega-N-methylarginine.
{ECO:0000244|PubMed:24129315}.
MOD_RES 1028 1028 Phosphoserine.
{ECO:0000244|PubMed:20068231,
ECO:0000244|PubMed:21406692,
ECO:0000244|PubMed:23186163}.
MOD_RES 1032 1032 Omega-N-methylarginine.
{ECO:0000244|PubMed:24129315}.
MOD_RES 1042 1042 Omega-N-methylarginine.
{ECO:0000244|PubMed:24129315}.
MOD_RES 1077 1077 Phosphoserine.
{ECO:0000244|PubMed:23186163}.
MOD_RES 1092 1092 Phosphoserine.
{ECO:0000244|PubMed:17924679,
ECO:0000244|PubMed:18669648,
ECO:0000244|PubMed:20068231,
ECO:0000244|PubMed:21406692,
ECO:0000244|PubMed:23186163}.
MOD_RES 1095 1095 N6-acetyllysine.
{ECO:0000244|PubMed:19608861}.
MOD_RES 1145 1145 Phosphoserine.
{ECO:0000244|PubMed:21406692,
ECO:0000244|PubMed:23186163}.
MOD_RES 1147 1147 Phosphoserine.
{ECO:0000244|PubMed:21406692,
ECO:0000244|PubMed:23186163}.
MOD_RES 1185 1185 Phosphoserine; by PKC/PRKCA.
{ECO:0000244|PubMed:20068231,
ECO:0000244|PubMed:21406692,
ECO:0000244|PubMed:23186163,
ECO:0000269|PubMed:21576361}.
MOD_RES 1187 1187 Phosphoserine.
{ECO:0000244|PubMed:20068231,
ECO:0000244|PubMed:21406692,
ECO:0000244|PubMed:23186163}.
MOD_RES 1194 1194 Phosphoserine.
{ECO:0000244|PubMed:23186163}.
MOD_RES 1209 1209 Phosphoserine.
{ECO:0000244|PubMed:18669648,
ECO:0000244|PubMed:20068231,
ECO:0000244|PubMed:21406692,
ECO:0000244|PubMed:23186163}.
MOD_RES 1211 1211 Phosphothreonine.
{ECO:0000244|PubMed:20068231,
ECO:0000244|PubMed:21406692}.
MOD_RES 1231 1231 Phosphoserine.
{ECO:0000244|PubMed:16964243,
ECO:0000244|PubMed:17081983,
ECO:0000244|PubMed:20068231,
ECO:0000244|PubMed:21406692,
ECO:0000244|PubMed:23186163}.
MOD_RES 1238 1238 Phosphoserine.
{ECO:0000244|PubMed:23186163}.
MOD_RES 1596 1596 Phosphoserine.
{ECO:0000244|PubMed:20068231,
ECO:0000244|PubMed:21406692,
ECO:0000244|PubMed:23186163}.
VAR_SEQ 1 196 Missing (in isoform E and isoform 7).
{ECO:0000303|PubMed:1429670}.
/FTId=VSP_018723.
VAR_SEQ 1 164 Missing (in isoform D). {ECO:0000305}.
/FTId=VSP_018722.
VAR_SEQ 1 87 Missing (in isoform C).
{ECO:0000303|PubMed:9418880}.
/FTId=VSP_018721.
VAR_SEQ 1 40 Missing (in isoform B).
{ECO:0000303|PubMed:9857202}.
/FTId=VSP_018720.
VAR_SEQ 48 48 R -> RQGGFRSL (in isoform 9).
{ECO:0000305}.
/FTId=VSP_047396.
VAR_SEQ 696 696 P -> PQ (in isoform 7 and isoform 8).
{ECO:0000303|PubMed:12052860,
ECO:0000303|PubMed:1429670,
ECO:0000303|PubMed:9372926,
ECO:0000303|Ref.12}.
/FTId=VSP_047397.
VARIANT 71 71 P -> S (in dbSNP:rs113810947).
{ECO:0000269|PubMed:21907011}.
/FTId=VAR_066571.
VARIANT 161 161 T -> A (in dbSNP:rs13319149).
{ECO:0000269|PubMed:12052860,
ECO:0000269|PubMed:17974005,
ECO:0000269|PubMed:21907011,
ECO:0000269|PubMed:9372926,
ECO:0000269|PubMed:9755181}.
/FTId=VAR_061147.
VARIANT 311 311 Y -> C (in dbSNP:rs16858632).
{ECO:0000269|PubMed:21907011}.
/FTId=VAR_055704.
VARIANT 432 432 M -> V (in dbSNP:rs2178403).
{ECO:0000244|PubMed:19413330,
ECO:0000269|PubMed:12052860,
ECO:0000269|PubMed:1429670,
ECO:0000269|PubMed:21907011,
ECO:0000269|PubMed:9372926}.
/FTId=VAR_063040.
VARIANT 466 468 Missing. {ECO:0000269|PubMed:21907011}.
/FTId=VAR_066572.
VARIANT 502 502 A -> V (in PARK18; dbSNP:rs111290936).
{ECO:0000269|PubMed:21907011}.
/FTId=VAR_066573.
VARIANT 686 686 G -> C (found in patients with Parkinson
disease; unknown pathological
significance; dbSNP:rs112019125).
{ECO:0000269|PubMed:21907011}.
/FTId=VAR_066574.
VARIANT 696 696 P -> L (in a colorectal cancer sample;
somatic mutation; dbSNP:rs754755344).
{ECO:0000269|PubMed:16959974}.
/FTId=VAR_036117.
VARIANT 806 806 I -> V (in dbSNP:rs62287499).
{ECO:0000269|PubMed:21907011}.
/FTId=VAR_066575.
VARIANT 829 829 T -> S (in dbSNP:rs111500185).
{ECO:0000269|PubMed:21907011}.
/FTId=VAR_066576.
VARIANT 1164 1164 S -> R (found in a patient with Parkinson
disease; unknown pathological
significance; dbSNP:rs113169049).
{ECO:0000269|PubMed:21907011}.
/FTId=VAR_066577.
VARIANT 1197 1197 R -> W (found in a patient with Parkinson
disease; unknown pathological
significance; dbSNP:rs113388242).
{ECO:0000269|PubMed:21907011}.
/FTId=VAR_066578.
VARIANT 1205 1205 R -> H (in PARK18; dbSNP:rs112176450).
{ECO:0000269|PubMed:21907011}.
/FTId=VAR_066579.
VARIANT 1229 1229 P -> A (in dbSNP:rs35629949).
{ECO:0000269|PubMed:21907011}.
/FTId=VAR_061148.
VARIANT 1233 1233 L -> P (in dbSNP:rs2230570).
{ECO:0000269|PubMed:21907011}.
/FTId=VAR_055705.
VARIANT 1257 1257 N -> S (in dbSNP:rs73053766).
{ECO:0000269|PubMed:21907011}.
/FTId=VAR_066580.
MUTAGEN 174 178 KRERK->AAAAA: Loss of PABPC1 binding;
when associated with 184-AAAA-187.
{ECO:0000269|PubMed:10996799}.
MUTAGEN 180 180 I->A: Loss of PABPC1 binding.
{ECO:0000269|PubMed:12086624}.
MUTAGEN 182 182 I->A: Loss of PABPC1 binding.
{ECO:0000269|PubMed:12086624}.
MUTAGEN 184 187 DPNQ->AAAA: Loss of PABPC1 binding; when
associated with 174-AAAAA-178.
MUTAGEN 192 192 I->A: Loss of PABPC1 binding.
{ECO:0000269|PubMed:12086624}.
MUTAGEN 196 196 I->A: Loss of PABPC1 binding.
{ECO:0000269|PubMed:12086624}.
MUTAGEN 612 612 Y->A,F: Abolishes binding to EIF4E.
{ECO:0000269|PubMed:7651417}.
MUTAGEN 617 618 LL->AA: Abolishes binding to EIF4E.
{ECO:0000269|PubMed:7651417}.
MUTAGEN 682 682 G->A,V,W,R,E: Reduced cleavage by
protease 2A from human rhinovirus 2.
{ECO:0000269|PubMed:8961935}.
MUTAGEN 768 768 L->A: Abolishes binding to EIF4A; when
associated with A-770 and A-775.
{ECO:0000269|PubMed:9372926}.
MUTAGEN 771 771 L->A: Abolishes binding to EIF4A; when
associated with A-767 and A-775.
{ECO:0000269|PubMed:9372926}.
MUTAGEN 776 776 F->A: Abolishes binding to EIF4A; when
associated with A-767 and A-770.
{ECO:0000269|PubMed:9372926}.
MUTAGEN 842 843 LL->AA: Abolishes binding to EIF4A; when
associated with A-850 and K-851.
{ECO:0000269|PubMed:9372926}.
MUTAGEN 851 852 FE->AK: Abolishes binding to EIF4A; when
associated with A-841 and A-842.
{ECO:0000269|PubMed:9372926}.
MUTAGEN 896 896 L->A: Abolishes binding to EIF4A; when
associated with A-92 and A-95.
{ECO:0000269|PubMed:9372926}.
MUTAGEN 902 902 I->A: Abolishes binding to EIF4A; when
associated with A-895 and A-95.
{ECO:0000269|PubMed:9372926}.
MUTAGEN 905 905 L->A: Abolishes binding to EIF4A; when
associated with A-895 and A-92.
{ECO:0000269|PubMed:9372926}.
MUTAGEN 974 974 R->A: Abolishes binding to EIF4A; when
associated with A-976.
{ECO:0000269|PubMed:9372926}.
MUTAGEN 977 977 F->A: Abolishes binding to EIF4A; when
associated with A-973.
{ECO:0000269|PubMed:9372926}.
MUTAGEN 985 985 L->A: Slightly reduced binding to EIF4A;
when associated with A-989.
{ECO:0000269|PubMed:9372926}.
MUTAGEN 990 990 W->A: Slightly reduced binding to EIF4A;
when associated with A-984.
{ECO:0000269|PubMed:9372926}.
CONFLICT 30 30 P -> R (in Ref. 9; AAC78443).
{ECO:0000305}.
CONFLICT 138 138 F -> L (in Ref. 5; AAL92872/AAM69365).
{ECO:0000305}.
CONFLICT 149 149 Q -> R (in Ref. 5; AAL92872/AAM69365).
{ECO:0000305}.
CONFLICT 214 214 G -> S (in Ref. 1; BAA02185).
{ECO:0000305}.
CONFLICT 462 462 E -> D (in Ref. 1; BAA02185).
{ECO:0000305}.
CONFLICT 468 468 A -> V (in Ref. 1; BAA02185).
{ECO:0000305}.
CONFLICT 474 474 A -> G (in Ref. 1; BAA02185).
{ECO:0000305}.
CONFLICT 479 479 G -> R (in Ref. 1; BAA02185).
{ECO:0000305}.
CONFLICT 604 604 L -> P (in Ref. 1; BAA02185, 5; AAL92872/
AAM69365 and 10; AAC82471).
{ECO:0000305}.
CONFLICT 625 626 AS -> CQ (in Ref. 1; BAA02185).
{ECO:0000305}.
CONFLICT 693 693 P -> A (in Ref. 1; BAA02185).
{ECO:0000305}.
CONFLICT 696 696 P -> A (in Ref. 1; BAA02185).
{ECO:0000305}.
CONFLICT 764 764 V -> W (in Ref. 1; BAA02185).
{ECO:0000305}.
CONFLICT 878 878 G -> E (in Ref. 1; BAA02185).
{ECO:0000305}.
CONFLICT 894 894 R -> C (in Ref. 1; BAA02185).
{ECO:0000305}.
CONFLICT 1104 1104 K -> Q (in Ref. 1; BAA02185).
{ECO:0000305}.
CONFLICT 1121 1121 N -> I (in Ref. 1; BAA02185).
{ECO:0000305}.
CONFLICT 1185 1185 S -> T (in Ref. 1; BAA02185).
{ECO:0000305}.
CONFLICT 1384 1384 C -> Y (in Ref. 6; CAI46013).
{ECO:0000305}.
CONFLICT 1472 1472 Missing (in Ref. 1; BAA02185).
{ECO:0000305}.
STRAND 181 183 {ECO:0000244|PDB:1LJ2}.
HELIX 185 187 {ECO:0000244|PDB:4F02}.
HELIX 193 197 {ECO:0000244|PDB:4F02}.
HELIX 614 618 {ECO:0000244|PDB:5T46}.
TURN 619 622 {ECO:0000244|PDB:5T46}.
HELIX 624 627 {ECO:0000244|PDB:5T46}.
TURN 637 639 {ECO:0000244|PDB:5T46}.
HELIX 1234 1256 {ECO:0000244|PDB:1UG3}.
HELIX 1259 1267 {ECO:0000244|PDB:1UG3}.
HELIX 1272 1274 {ECO:0000244|PDB:1UG3}.
HELIX 1275 1286 {ECO:0000244|PDB:1UG3}.
TURN 1287 1289 {ECO:0000244|PDB:1UG3}.
HELIX 1291 1306 {ECO:0000244|PDB:1UG3}.
HELIX 1312 1329 {ECO:0000244|PDB:1UG3}.
TURN 1330 1332 {ECO:0000244|PDB:1UG3}.
HELIX 1336 1344 {ECO:0000244|PDB:1UG3}.
HELIX 1345 1348 {ECO:0000244|PDB:1UG3}.
HELIX 1355 1362 {ECO:0000244|PDB:1UG3}.
TURN 1363 1365 {ECO:0000244|PDB:1UG3}.
HELIX 1366 1369 {ECO:0000244|PDB:1UG3}.
HELIX 1372 1387 {ECO:0000244|PDB:1UG3}.
HELIX 1389 1398 {ECO:0000244|PDB:1UG3}.
HELIX 1403 1405 {ECO:0000244|PDB:1UG3}.
HELIX 1413 1419 {ECO:0000244|PDB:1UG3}.
HELIX 1423 1425 {ECO:0000244|PDB:1UG3}.
HELIX 1439 1452 {ECO:0000244|PDB:1UG3}.
HELIX 1457 1467 {ECO:0000244|PDB:1UG3}.
HELIX 1470 1473 {ECO:0000244|PDB:1UG3}.
HELIX 1476 1489 {ECO:0000244|PDB:1UG3}.
STRAND 1494 1496 {ECO:0000244|PDB:1UG3}.
HELIX 1501 1514 {ECO:0000244|PDB:1UG3}.
HELIX 1518 1534 {ECO:0000244|PDB:1UG3}.
HELIX 1541 1551 {ECO:0000244|PDB:1UG3}.
HELIX 1557 1563 {ECO:0000244|PDB:1UG3}.
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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