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UniProtKB/Swiss-Prot entry Q04637

[Entry info] [Name and origin] [References] [Comments] [Cross-references] [Keywords] [Features] [Sequence] [Tools]

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Entry information
Entry name IF4G1_HUMAN
Primary accession number Q04637
Secondary accession numbers O43177 O95066 Q5HYG0 Q6ZN21 Q8N102
Integrated into Swiss-Prot on February 1, 1995
Sequence was last modified on January 16, 2004 (Sequence version 3)
Annotations were last modified on    July 22, 2008 (Entry version 94)
Name and origin of the protein
Protein name Eukaryotic translation initiation factor 4 gamma 1
Synonyms eIF-4-gamma 1
eIF-4G 1
eIF-4G1
p220
Gene name
Name: EIF4G1
Synonyms: EIF4F, EIF4G, EIF4GI
From
Homo sapiens (Human) [TaxID: 9606] 
Taxonomy Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini; Hominidae; Homo.
Protein existence 1: Evidence at protein level;
References
[1]
 NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM E).
TISSUE=Brain;
PubMed=1429670 [NCBI, ExPASy, EBI, Israel, Japan]
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 E), INTERACTION WITH EIF4A, AND MUTAGENESIS OF LEU-769; LEU-772; PHE-777; 843-LEU-LEU-844; 852-PHE-GLU-852; LEU-897; ILE-903; LEU-906; ARG-975; PHE-978; LEU-986 AND TRP-991.
PubMed=9372926 [NCBI, ExPASy, EBI, Israel, Japan]
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).
[3]
 NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM B), AND INTERACTION WITH PABPC1.
DOI=10.1093/emboj/17.24.7480; PubMed=9857202 [NCBI, ExPASy, EBI, Israel, Japan]
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).
[4]
 NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM C).
PubMed=9418880 [NCBI, ExPASy, EBI, Israel, Japan]
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).
[5]
 NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM A), AND ALTERNATIVE INITIATION.
DOI=10.1128/MCB.22.13.4499-4511.2002; PubMed=12052860 [NCBI, ExPASy, EBI, Israel, Japan]
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).
[6]
 NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 2).
DOI=10.1038/ng1285; PubMed=14702039 [NCBI, ExPASy, EBI, Israel, Japan]
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).
[7]
 NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM A).
TISSUE=Endometrial tumor;
The German cDNA consortium;
Submitted (JAN-2005) to the EMBL/GenBank/DDBJ databases.
[8]
 NUCLEOTIDE SEQUENCE [MRNA] OF 30-206, NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 180-234, AND INTERACTION WITH ROTAVIRAL NSP3.
DOI=10.1093/emboj/17.19.5811; PubMed=9755181 [NCBI, ExPASy, EBI, Israel, Japan]
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).
[9]
 NUCLEOTIDE SEQUENCE [MRNA] OF 605-722, INTERACTION WITH EIF4E, AND MUTAGENESIS OF TYR-612 AND 617-LEU-LEU-618.
PubMed=7651417 [NCBI, ExPASy, EBI, Israel, Japan]
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).
[10]
 NUCLEOTIDE SEQUENCE [MRNA] OF 682-913.
De Gregorio E.;
Submitted (AUG-1997) to the EMBL/GenBank/DDBJ databases.
[11]
 CLEAVAGE BY RHINOVIRUS AND COXSACKIEVIRUS PROTEASE.
PubMed=8396129 [NCBI, ExPASy, EBI, Israel, Japan]
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).
[12]
 INTERACTION WITH EIF4E.
TISSUE=Placenta;
DOI=10.1038/371762a0; PubMed=7935836 [NCBI, ExPASy, EBI, Israel, Japan]
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).
[13]
 INTERACTION WITH EIF4E AND EIF4EBP1.
PubMed=8521827 [NCBI, ExPASy, EBI, Israel, Japan]
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).
[14]
 MUTAGENESIS OF GLY-682.
DOI=10.1021/bi961864t; PubMed=8961935 [NCBI, ExPASy, EBI, Israel, Japan]
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).
[15]
 CLEAVAGE BY POLIOVIRUS.
DOI=10.1016/S0014-5793(98)01027-8; PubMed=9755863 [NCBI, ExPASy, EBI, Israel, Japan]
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).
[16]
 REVIEW.
DOI=10.1146/annurev.biochem.68.1.913; PubMed=10872469 [NCBI, ExPASy, EBI, Israel, Japan]
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).
[17]
 INTERACTION WITH MKNK1.
DOI=10.1093/emboj/18.1.270; PubMed=9878069 [NCBI, ExPASy, EBI, Israel, Japan]
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).
[18]
 INTERACTION WITH PABPC1, AND MUTAGENESIS OF 174-LYS--LYS-178 AND 184-ASP--GLN-197.
DOI=10.1016/S0960-9822(00)00701-6; PubMed=10996799 [NCBI, ExPASy, EBI, Israel, Japan]
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).
[19]
 INTERACTION WITH PABPC1.
DOI=10.1093/emboj/19.17.4723; PubMed=10970864 [NCBI, ExPASy, EBI, Israel, Japan]
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).
[20]
 CLEAVAGE BY FMDV AND HRV-2.
DOI=10.1016/S0014-5793(00)01928-1; PubMed=11034318 [NCBI, ExPASy, EBI, Israel, Japan]
Glaser W., Skern T.;
"Extremely efficient cleavage of eIF4G by picornaviral proteinases L and 2A in vitro.";
FEBS Lett. 480:151-155(2000).
[21]
 INTERACTION WITH MKNK2.
DOI=10.1128/MCB.21.3.743-754.2001; PubMed=11154262 [NCBI, ExPASy, EBI, Israel, Japan]
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).
[22]
 PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-1210 AND SER-1232, AND MASS SPECTROMETRY.
TISSUE=Epithelium;
DOI=10.1073/pnas.0404720101; PubMed=15302935 [NCBI, ExPASy, EBI, Israel, Japan]
Beausoleil S.A., Jedrychowski M., Schwartz D., Elias J.E., Villen J., Li J., Cohn M.A., Cantley L.C., Gygi S.P.;
"Large-scale characterization of HeLa cell nuclear phosphoproteins.";
Proc. Natl. Acad. Sci. U.S.A. 101:12130-12135(2004).
[23]
 PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT TYR-594, AND MASS SPECTROMETRY.
DOI=10.1038/nbt1046; PubMed=15592455 [NCBI, ExPASy, EBI, Israel, Japan]
Rush J., Moritz A., Lee K.A., Guo A., Goss V.L., Spek E.J., Zhang H., Zha X.-M., Polakiewicz R.D., Comb M.J.;
"Immunoaffinity profiling of tyrosine phosphorylation in cancer cells.";
Nat. Biotechnol. 23:94-101(2005).
[24]
 PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-1146; SER-1148; SER-1186 AND SER-1232, AND MASS SPECTROMETRY.
TISSUE=Epithelium;
DOI=10.1016/j.cell.2006.09.026; PubMed=17081983 [NCBI, ExPASy, EBI, Israel, Japan]
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).
[25]
 PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-1232, AND MASS SPECTROMETRY.
TISSUE=Epithelium;
DOI=10.1038/nbt1240; PubMed=16964243 [NCBI, ExPASy, EBI, Israel, Japan]
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).
[26]
 PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-1093 AND SER-1232, AND MASS SPECTROMETRY.
TISSUE=Epithelium;
DOI=10.1021/pr070152u; PubMed=17924679 [NCBI, ExPASy, EBI, Israel, Japan]
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).
[27]
 PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-1210, AND MASS SPECTROMETRY.
DOI=10.1073/pnas.0611217104; PubMed=17287340 [NCBI, ExPASy, EBI, Israel, Japan]
Molina H., Horn D.M., Tang N., Mathivanan S., Pandey A.;
"Global proteomic profiling of phosphopeptides using electron transfer dissociation tandem mass spectrometry.";
Proc. Natl. Acad. Sci. U.S.A. 104:2199-2204(2007).
[28]
 PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-1232, AND MASS SPECTROMETRY.
DOI=10.2116/analsci.24.161; PubMed=18187866 [NCBI, ExPASy, EBI, Israel, Japan]
Imami K., Sugiyama N., Kyono Y., Tomita M., Ishihama Y.;
"Automated phosphoproteome analysis for cultured cancer cells by two-dimensional nanoLC-MS using a calcined titania/C18 biphasic column.";
Anal. Sci. 24:161-166(2008).
[29]
 PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-1210, AND MASS SPECTROMETRY.
TISSUE=Platelet;
DOI=10.1021/pr0704130; PubMed=18088087 [NCBI, ExPASy, EBI, Israel, Japan]
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).
[30]
 INTERACTION WITH MIF4GD.
DOI=10.1128/MCB.01500-07; PubMed=18025107 [NCBI, ExPASy, EBI, Israel, Japan]
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).
[31]
 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.
DOI=10.1016/S1097-2765(02)00555-5; PubMed=12086624 [NCBI, ExPASy, EBI, Israel, Japan]
Groft C.M., Burley S.K.;
"Recognition of eIF4G by rotavirus NSP3 reveals a basis for mRNA circularization.";
Mol. Cell 9:1273-1283(2002).
[32]
 X-RAY CRYSTALLOGRAPHY (2.24 ANGSTROMS) OF 1235-1572.
DOI=10.1016/j.str.2006.03.012; PubMed=16698552 [NCBI, ExPASy, EBI, Israel, Japan]
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).
[33]
 VARIANT [LARGE SCALE ANALYSIS] LEU-696.
DOI=10.1126/science.1133427; PubMed=16959974 [NCBI, ExPASy, EBI, Israel, Japan]
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).
Comments
  • 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 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. During rotaviral infection, rotavirus RNA-binding protein NSP3 interacts with EIF4G1 and takes the place of PABPC1. Rapamycin can attenuate insulin stimulation mediated by FKBPs. Interacts with EIF4E3. Interacts with MIF4GD.
  • INTERACTION:
    P60842:EIF4A1; NbExp=3; IntAct=EBI-73711, EBI-73449;
    Q14240:EIF4A2; NbExp=2; IntAct=EBI-73711, EBI-73473;
    P06730:EIF4E; NbExp=1; IntAct=EBI-73711, EBI-73440;
    Q8BMB3:Eif4e2 (xeno); NbExp=1; IntAct=EBI-73711, EBI-398682;
    P60520:GABARAPL2; NbExp=1; IntAct=EBI-73711, EBI-720116;
    Q14103-1:HNRPD; NbExp=1; IntAct=EBI-73711, EBI-432527;
    Q14103-2:HNRPD; NbExp=1; IntAct=EBI-73711, EBI-432533;
    Q14103-3:HNRPD; NbExp=1; IntAct=EBI-73711, EBI-432539;
    Q14103-4:HNRPD; NbExp=1; IntAct=EBI-73711, EBI-432545;
    P43360:MAGEA6; NbExp=1; IntAct=EBI-73711, EBI-1045155;
    Q9BUB5:MKNK1; NbExp=1; IntAct=EBI-73711, EBI-73837;
    P11940:PABPC1; NbExp=1; IntAct=EBI-73711, EBI-81531;
    Q53EL6:PDCD4; NbExp=1; IntAct=EBI-73711, EBI-935824;
    P03536:S7 (xeno); NbExp=1; IntAct=EBI-73711, EBI-296448;
  • ALTERNATIVE PRODUCTS: 6 named isoforms [FASTA] produced by alternative splicing and alternative initiation.
    Name1
    SynonymsA
    Isoform IDQ04637-1
    This is the isoform sequence displayed in this entry.
    Name2
    Isoform IDQ04637-2
    Note: No experimental confirmation available.
    Features which should be applied to build the isoform sequence: VSP_013973.
    NameB
    Isoform IDQ04637-3
    Note: Produced by alternative initiation at Met-41 of isoform 1.
    Features which should be applied to build the isoform sequence: VSP_018720.
    NameC
    Isoform IDQ04637-4
    Note: Produced by alternative initiation at Met-88 of isoform 1.
    Features which should be applied to build the isoform sequence: VSP_018721.
    NameD
    Isoform IDQ04637-5
    Note: Produced by alternative initiation at Met-165 of isoform 1.
    Features which should be applied to build the isoform sequence: VSP_018722.
    NameE
    Isoform IDQ04637-6
    Note: Produced by alternative initiation at Met-197 of isoform 1.
    Features which should be applied to build the isoform sequence: VSP_018723.
  • PTM: Phosphorylated at multiple sites in vivo.
  • 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.
  • SIMILARITY: Belongs to the eIF4G family.
  • SIMILARITY: Contains 1 MI domain.
  • SIMILARITY: Contains 1 MIF4G domain.
  • SIMILARITY: Contains 1 W2 domain.
  • SEQUENCE CAUTION:
    • Sequence=BAA02185.1; Type=Frameshift; Positions=Several;
Copyright
Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms. Distributed under the Creative Commons Attribution-NoDerivs License.
Cross-references
Sequence databases
EMBL
D12686; BAA02185.1; ALT_FRAME; mRNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
AF104913; AAC82471.1; ALT_INIT; mRNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
AY082886; AAL92872.1; -; mRNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
AF281070; AAM69365.1; -; mRNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
AK131407; BAD18554.1; -; mRNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
BX647812; CAI46013.1; -; mRNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
AF002816; AAC78443.1; -; mRNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
AF004836; AAC78444.1; ALT_INIT; Genomic_DNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
AJ001046; CAA04500.1; -; mRNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
PIR A44453; A44453.
RefSeq NP_937884.1; -.
UniGene Hs.433750
3D structure databases
PDB
1LJ2; X-ray; 2.38 A; C/D=172-199.[ExPASy / RCSB / EBI]
1UG3; X-ray; 2.24 A; A/B=1234-1572.[ExPASy / RCSB / EBI]
Detailed list of linked structures.
PDBsum 1LJ2; -.
1UG3; -.
SMR Q04637; 752-992.
ModBase Q04637.
Protein-protein interaction databases
DIP DIP:1161N; -.
IntAct Q04637; -.
PTM databases
PhosphoSite Q04637; -.
Enzyme and pathway databases
Reactome REACT_1762; 3' -UTR-mediated translational regulation.
REACT_498; Signaling by insulin receptor.
REACT_71; Gene Expression.
Organism-specific databases
H-InvDB HIX0003910; -.
HGNC HGNC:3296; EIF4G1.
GenAtlas EIF4G1.
HPA CAB014774; -.
MIM 600495; gene. [NCBI / EBI]
PharmGKB PA27722; -.
GeneCards Q04637.
Gene expression databases
ArrayExpress Q04637; -.
CleanEx HS_EIF4G1; -.
GermOnline ENSG00000114867; Homo sapiens.
Ontologies
GO
GO:0005829; Cellular component: cytosol (inferred from experiment from Reactome).
GO:0016281; Cellular component: eukaryotic translation initiation factor 4F complex (traceable author statement from ProtInc).
GO:0005515; Molecular function: protein binding (inferred from physical interaction from UniProtKB).
GO:0003743; Molecular function: translation initiation factor activity (traceable author statement from UniProtKB).
GO:0006446; Biological process: regulation of translational initiation (non-traceable author statement from UniProtKB).
QuickGo view.
Family and domain databases
InterPro IPR003307; eIF5C.
IPR003891; IF_eIF4G_MA3.
IPR016021; MIF4-like_typ_1/2/3.
IPR003890; MIF4G-like_typ-3.
Graphical view of domain structure.
Gene3D G3DSA:1.25.40.230; eIF5C; 1.
G3DSA:1.25.40.180; MIF4-like_typ_1/2/3; 1.
Pfam PF02847; MA3; 1.
PF02854; MIF4G; 1.
PF02020; W2; 1.
Pfam graphical view of domain structure.
SMART SM00515; eIF5C; 1.
SM00544; MA3; 1.
SM00543; MIF4G; 1.
SMART graphical view of domain structure.
PROSITE PS51366; MI; 1.
PS51363; W2; 1.
PROSITE graphical view of domain structure (profiles).
BLOCKS Q04637.
Genome annotation databases
Ensembl ENSG00000114867; Homo sapiens. [Contig view]
GeneID 1981; -.
Phylogenomic databases
HOVERGEN Q04637; -.
Other
SOURCE EIF4G1; Homo sapiens.
ProtoNet Q04637.
UniRef View cluster of proteins with at least 50% / 90% / 100% identity.
Keywords
3D-structure; Alternative initiation; Alternative splicing; Host-virus interaction; Initiation factor; Phosphoprotein; Polymorphism; Protein biosynthesis; RNA-binding; Translation regulation.
Features
SEVIEWER logo Feature table viewer FT aligner logo Feature aligner
KeyFrom    To Length Description FTId
CHAIN   1   1600  1600     Eukaryotic translation initiation factor 4 gamma 1. PRO_0000007786
DOMAIN   565    792  228     MIF4G. 
DOMAIN   1242   1364  123     MI. 
DOMAIN   1434   1600  167     W2. 
REGION   172    200  29     PABPC1-binding. 
REGION   607    618  12     EIF4E-binding. 
REGION   682   1086  405     eIF3/EIF4A-binding. 
REGION   1451   1600  150     EIF4A-binding. 
REGION   1586   1600  15     Necessary but not sufficient for MKNK1-binding. 
COMPBIAS   454    467  14     Poly-Glu. 
COMPBIAS   501    504  4     Poly-Ala. 
SITE   674    675  2     Cleavage; by foot-and-mouth disease virus leader protease. 
SITE   681    682  2     Cleavage; by enterovirus/rhinovirus protease 2A. 
MOD_RES   205    205        Phosphothreonine (By similarity). 
MOD_RES   207    207        Phosphothreonine (By similarity). 
MOD_RES   594    594        Phosphotyrosine. 
MOD_RES   1093   1093        Phosphoserine. 
MOD_RES   1146   1146        Phosphoserine. 
MOD_RES   1148   1148        Phosphoserine. 
MOD_RES   1186   1186        Phosphoserine. 
MOD_RES   1210   1210        Phosphoserine. 
MOD_RES   1232   1232        Phosphoserine. 
VAR_SEQ   1    196        Missing (in isoform E). VSP_018723
VAR_SEQ   1    164        Missing (in isoform D). VSP_018722
VAR_SEQ   1     87        Missing (in isoform C). VSP_018721
VAR_SEQ   1     40        Missing (in isoform B). VSP_018720
VAR_SEQ   77   1225        Missing (in isoform 2). VSP_013973
VARIANT   696    696  1     P -> L (in a colorectal cancer sample; somatic mutation). VAR_036117 
MUTAGEN   174    178        KRERK->AAAAA: Loss of PABPC1 binding; when associated with 184-AAAA-187. 
MUTAGEN   180    180        I->A: Loss of PABPC1 binding. 
MUTAGEN   182    182        I->A: Loss of PABPC1 binding. 
MUTAGEN   184    187        DPNQ->AAAA: Loss of PABPC1 binding; when associated with 174-AAAAA-178. 
MUTAGEN   192    192        I->A: Loss of PABPC1 binding. 
MUTAGEN   196    196        I->A: Loss of PABPC1 binding. 
MUTAGEN   612    612        Y->A,F: Abolishes binding to EIF4E. 
MUTAGEN   617    618        LL->AA: Abolishes binding to EIF4E. 
MUTAGEN   682    682        G->A,V,W,R,E: Reduced cleavage by protease 2A from human rhinovirus 2. 
MUTAGEN   769    769        L->A: Abolishes binding to EIF4A; when associated with A-772 and A-777. 
MUTAGEN   772    772        L->A: Abolishes binding to EIF4A; when associated with A-769 and A-777. 
MUTAGEN   777    777     &nbs