[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 A). 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; DOI=10.1186/1471-2164-8-399; PubMed=17974005 [NCBI, ExPASy, EBI, Israel, Japan] Bechtel S., Rosenfelder H., Duda A., Schmidt C.P., Ernst U., Wellenreuther R., Mehrle A., Schuster C., Bahr A., Blocker H., Heubner D., Hoerlein A., Michel G., Wedler H., Kohrer K., Ottenwalder B., Poustka A., Wiemann S., Schupp I.; "The full-ORF clone resource of the German cDNA consortium."; BMC Genomics 8:399-399(2007).
[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 ROTAVIRUS A NSP3. DOI=10.1128/JVI.00872-08; PubMed=18799579 [NCBI, ExPASy, EBI, Israel, Japan] 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).
[31]	PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-1232, AND MASS SPECTROMETRY. DOI=10.1016/j.molcel.2008.07.007; PubMed=18691976 [NCBI, ExPASy, EBI, Israel, Japan] Daub H., Olsen J.V., Bairlein M., Gnad F., Oppermann F.S., Korner R., Greff Z., Keri G., Stemmann O., Mann M.; "Kinase-selective enrichment enables quantitative phosphoproteomics of the kinome across the cell cycle."; Mol. Cell 31:438-448(2008).
[32]	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).
[33]	PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-205; THR-207; THR-223; THR-647; SER-1093; SER-1186; SER-1188; SER-1210; SER-1232 AND SER-1597, AND MASS SPECTROMETRY. DOI=10.1073/pnas.0805139105; PubMed=18669648 [NCBI, ExPASy, EBI, Israel, Japan] 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 [LARGE SCALE ANALYSIS], AND MASS SPECTROMETRY. Colinge J., Superti-Furga G., Bennett K.L.; Submitted (OCT-2008) to UniProtKB.
[35]	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).
[36]	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).
[37]	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. Rapamycin can attenuate insulin stimulation mediated by FKBPs. Interacts with EIF4E3. Interacts with MIF4GD. Interacts with rotavirus A NSP3; in this interaction, NSP3 takes the place of PABPC1 thereby inducing shutoff of host protein synthesis.
INTERACTION:
P03536:- (xeno); NbExp=1; IntAct=EBI-73711, EBI-296448;
P60842:EIF4A1; NbExp=5; IntAct=EBI-73711, EBI-73449;
Q14240:EIF4A2; NbExp=3; 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:HNRNPD; NbExp=1; IntAct=EBI-73711, EBI-432527;
Q14103-2:HNRNPD; NbExp=1; IntAct=EBI-73711, EBI-432533;
Q14103-3:HNRNPD; NbExp=1; IntAct=EBI-73711, EBI-432539;
Q14103-4:HNRNPD; 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;

ALTERNATIVE PRODUCTS: 5 named isoforms [FASTA] produced by alternative splicing and alternative initiation.

Name	1
Synonyms	A
Isoform ID	Q04637-1
This is the isoform sequence displayed in this entry.

Name	B
Isoform ID	Q04637-3
Note: Produced by alternative initiation at Met-41 of isoform 1.
Features which should be applied to build the isoform sequence: VSP_018720.

Name	C
Isoform ID	Q04637-4
Note: Produced by alternative initiation at Met-88 of isoform 1.
Features which should be applied to build the isoform sequence: VSP_018721.

Name	D
Isoform ID	Q04637-5
Note: Produced by alternative initiation at Met-165 of isoform 1.
Features which should be applied to build the isoform sequence: VSP_018722.

Name	E
Isoform ID	Q04637-6
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;
- Sequence=BAD18554.1; Type=Miscellaneous discrepancy; Note=Aberrant splicing

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; ALT_SEQ; 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]

IPI

IPI00479262; -.
IPI00552639; -.
IPI00759560; -.
IPI00927510; -.
IPI00927765; -.

A44453; A44453.

NP_937884.1; -.

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=1235-1572.	[ExPASy / RCSB / EBI]

Detailed list of linked structures.

1LJ2; -.
1UG3; -.

Q04637; 752-992.

Protein-protein interaction databases

DIP

DIP:1161N; -.

IntAct

Q04637; 32.

PTM databases

PhosphoSite

Q04637; -.

Enzyme and pathway databases

Pathway_Interaction_DB

mtor_4pathway; mTOR signaling pathway.

Reactome

REACT_1762; 3' -UTR-mediated translational regulation.
REACT_498; Signaling by Insulin receptor.
REACT_71; Gene Expression.

Organism-specific databases

GC03P185515; -.

HIX0003910; -.

HGNC:3296; EIF4G1.

CAB014774; -.

600495; gene. [NCBI / EBI]

PharmGKB

PA27722; -.

Gene expression databases

Q04637; -.

Q04637; -.

HS_EIF4G1; -.

ENSG00000114867; Homo sapiens.

Ontologies

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:0003723;	Molecular function: RNA binding (inferred from electronic annotation from UniProtKB-KW).
GO:0003743;	Molecular function: translation initiation factor activity (traceable author statement from UniProtKB).
GO:0044419;	Biological process: interspecies interaction between organisms (inferred from electronic annotation from UniProtKB-KW).
GO:0006446;	Biological process: regulation of translational initiation (non-traceable author statement from UniProtKB).
GO:0016070;	Biological process: RNA metabolic process (inferred from electronic annotation from InterPro).
GO:0006412;	Biological process: translation (inferred from electronic annotation from UniProtKB-KW).
QuickGo view.

Family and domain databases

InterPro

IPR003307; eIF5C.
IPR003891; Initiation_fac_eIF4g_MI.
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).

Proteomic databases

PRIDE

Q04637; -.

Genome annotation databases

Ensembl

ENSG00000114867; Homo sapiens. [Contig view]

GeneID

1981; -.

Phylogenomic databases

HOVERGEN

Q04637; -.

Other

NextBio

8013; -.

PMAP-CutDB

Q04637; -.

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

Feature table viewer

Feature aligner

`Key`	`From 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.`
`MOD_RES`	`207 207`		`Phosphothreonine.`
`MOD_RES`	`223 223`		`Phosphothreonine.`
`MOD_RES`	`594 594`		`Phosphotyrosine.`
`MOD_RES`	`647 647`		`Phosphothreonine.`
`MOD_RES`	`1093 1093`		`Phosphoserine.`
`MOD_RES`	`1146 1146`		`Phosphoserine.`
`MOD_RES`	`1148 1148`		`Phosphoserine.`
`MOD_RES`	`1186 1186`		`Phosphoserine.`
`MOD_RES`	`1188 1188`		`Phosphoserine.`
`MOD_RES`	`1210 1210`		`Phosphoserine.`
`MOD_RES`	`1232 1232`		`Phosphoserine.`
`MOD_RES`	`1597 1597`		`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`
`VARIANT`	`311 311`	`1`	`Y -> C (in dbSNP:rs16858632 [NCBI]).`	`VAR_055704`
`VARIANT`	`696 696`	`1`	`P -> L (in a colorectal cancer sample; somatic mutation).`	`VAR_036117`
`VARIANT`	`1234 1234`	`1`	`L -> P (in dbSNP:rs2230570 [NCBI]).`	`VAR_055705`
`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`		`F->A: Abolishes binding to EIF4A; when associated with A-769 and A-772.`
`MUTAGEN`	`843 844`		`LL->AA: Abolishes binding to EIF4A; when associated with A-852 and K-853.`
`MUTAGEN`	`852 853`		`FE->AK: Abolishes binding to EIF4A; when associated with A-843 and A-844.`
`MUTAGEN`	`897 897`		`L->A: Abolishes binding to EIF4A; when associated with A-903 and A-906.`
`MUTAGEN`	`903 903`		`I->A: Abolishes binding to EIF4A; when associated with A-897 and A-906.`
`MUTAGEN`	`906 906`		`L->A: Abolishes binding to EIF4A; when associated with A-897 and A-903.`
`MUTAGEN`	`975 975`		`R->A: Abolishes binding to EIF4A; when associated with A-978.`
`MUTAGEN`	`978 978`		`F->A: Abolishes binding to EIF4A; when associated with A-975.`
`MUTAGEN`	`986 986`		`L->A: Slightly reduced binding to EIF4A; when associated with A-991.`
`MUTAGEN`	`991 991`		`W->A: Slightly reduced binding to EIF4A; when associated with A-986.`
`CONFLICT`	`30 30`		`P -> R (in Ref. 8; AAC78443).`
`CONFLICT`	`138 138`		`L -> F (in Ref. 3, 7 and 8; AAC78443).`
`CONFLICT`	`149 149`		`R -> Q (in Ref. 3, 7 and 8; AAC78443).`
`CONFLICT`	`214 214`		`G -> S (in Ref. 4; BAA02185).`
`CONFLICT`	`432 432`		`V -> M (in Ref. 7; CAI46013).`
`CONFLICT`	`462 462`		`E -> D (in Ref. 4; BAA02185).`
`CONFLICT`	`468 468`		`A -> V (in Ref. 4; BAA02185).`
`CONFLICT`	`474 474`		`A -> G (in Ref. 4; BAA02185).`
`CONFLICT`	`479 479`		`G -> R (in Ref. 4; BAA02185).`
`CONFLICT`	`604 604`		`P -> L (in Ref. 7; CAI46013).`
`CONFLICT`	`625 626`		`AS -> CQ (in Ref. 4; BAA02185).`
`CONFLICT`	`697 697`		`Missing (in Ref. 4 and 7).`
`CONFLICT`	`765 765`		`V -> W (in Ref. 4; BAA02185).`
`CONFLICT`	`879 879`		`G -> E (in Ref. 4; BAA02185).`
`CONFLICT`	`895 895`		`R -> C (in Ref. 4; BAA02185).`
`CONFLICT`	`1105 1105`		`K -> Q (in Ref. 4; BAA02185).`
`CONFLICT`	`1122 1122`		`N -> I (in Ref. 4; BAA02185).`
`CONFLICT`	`1186 1186`		`S -> T (in Ref. 4; BAA02185).`
`CONFLICT`	`1385 1385`		`C -> Y (in Ref. 7; CAI46013).`
`CONFLICT`	`1472 1472`		`Missing (in Ref. 4; BAA02185).`
`STRAND`	`181 183`	`3`
`HELIX`	`185 187`	`3`
`HELIX`	`193 196`	`4`
`HELIX`	`1235 1257`	`23`
`HELIX`	`1260 1268`	`9`
`HELIX`	`1273 1275`	`3`
`HELIX`	`1276 1287`	`12`
`TURN`	`1288 1290`	`3`
`HELIX`	`1292 1307`	`16`
`HELIX`	`1313 1330`	`18`
`TURN`	`1331 1333`	`3`
`HELIX`	`1337 1345`	`9`
`HELIX`	`1346 1349`	`4`
`HELIX`	`1356 1363`	`8`
`TURN`	`1364 1366`	`3`
`HELIX`	`1367 1370`	`4`
`HELIX`	`1373 1388`	`16`
`HELIX`	`1390 1399`	`10`
`HELIX`	`1404 1406`	`3`
`HELIX`	`1414 1420`	`7`
`HELIX`	`1424 1426`	`3`
`HELIX`	`1440 1453`	`14`
`HELIX`	`1458 1468`	`11`
`HELIX`	`1471 1474`	`4`
`HELIX`	`1477 1490`	`14`
`STRAND`	`1495 1497`	`3`
`HELIX`	`1502 1515`	`14`
`HELIX`	`1519 1535`	`17`
`HELIX`	`1542 1552`	`11`
`HELIX`	`1558 1564`	`7`

Sequence information

Length: 1600 AA [This is the length of the unprocessed precursor]

Molecular weight: 175535 Da [This is the MW of the unprocessed precursor]

CRC64: 9D9B058A9939AD1E [This is a checksum on the sequence]

        10         20         30         40         50         60 
MNKAPQSTGP PPAPSPGLPQ PAFPPGQTAP VVFSTPQATQ MNTPSQPRQH FYPSRAQPPS 

        70         80         90        100        110        120 
SAASRVQSAA PARPGPAAHV YPAGSQVMMI PSQISYPASQ GAYYIPGQGR STYVVPTQQY 

       130        140        150        160        170        180 
PVQPGAPGFY PGASPTELGT YAGAYYPARG VQQFPTGVAP APVLMNQPPQ IAPKRERKTI 

       190        200        210        220        230        240 
RIRDPNQGGK DITEEIMSGA RTASTPTPPQ TGGGLEPQAN GETPQVAVIV RPDDRSQGAI 

       250        260        270        280        290        300 
IADRPGLPGP EHSPSESQPS SPSPTPSPSP VLEPGSEPNL AVLSIPGDTM TTIQMSVEES 

       310        320        330        340        350        360 
TPISRETGEP YRLSPEPTPL AEPILEVEVT LSKPVPESEF SSSPLQAPTP LASHTVEIHE 

       370        380        390        400        410        420 
PNGMVPSEDL EPEVESSPEL APPPACPSES PVPIAPTAQP EELLNGAPSP PAVDLSPVSE 

       430        440        450        460        470        480 
PEEQAKEVTA SVAPPTIPSA TPATAPSATS PAQEEEMEEE EEEEEGEAGE AGEAESEKGG 

       490        500        510        520        530        540 
EELLPPESTP IPANLSQNLE AAAATQVAVS VPKRRRKIKE LNKKEAVGDL LDAFKEANPA 

       550        560        570        580        590        600 
VPEVENQPPA GSNPGPESEG SGVPPRPEEA DETWDSKEDK IHNAENIQPG EQKYEYKSDQ 

       610        620        630        640        650        660 
WKPPNLEEKK RYDREFLLGF QFIFASMQKP EGLPHISDVV LDKANKTPLR PLDPTRLQGI 

       670        680        690        700        710        720 
NCGPDFTPSF ANLGRTTLST RGPPRGGPGG ELPRGPQAGL GPRRSQQGPR KEPRKIIATV 

       730        740        750        760        770        780 
LMTEDIKLNK AEKAWKPSSK RTAADKDRGE EDADGSKTQD LFRRVRSILN KLTPQMFQQL 

       790        800        810        820        830        840 
MKQVTQLAID TEERLKGVID LIFEKAISEP NFSVAYANMC RCLMALKVPT TEKPTVTVNF 

       850        860        870        880        890        900 
RKLLLNRCQK EFEKDKDDDE VFEKKQKEMD EAATAEERGR LKEELEEARD IARRRSLGNI 

       910        920        930        940        950        960 
KFIGELFKLK MLTEAIMHDC VVKLLKNHDE ESLECLCRLL TTIGKDLDFE KAKPRMDQYF 

       970        980        990       1000       1010       1020 
NQMEKIIKEK KTSSRIRFML QDVLDLRGSN WVPRRGDQGP KTIDQIHKEA EMEEHREHIK 

      1030       1040       1050       1060       1070       1080 
VQQLMAKGSD KRRGGPPGPP ISRGLPLVDD GGWNTVPISK GSRPIDTSRL TKITKPGSID 

      1090       1100       1110       1120       1130       1140 
SNNQLFAPGG RLSWGKGSSG GSGAKPSDAA SEAARPATST LNRFSALQQA VPTESTDNRR 

      1150       1160       1170       1180       1190       1200 
VVQRSSLSRE RGEKAGDRGD RLERSERGGD RGDRLDRART PATKRSFSKE VEERSRERPS 

      1210       1220       1230       1240       1250       1260 
QPEGLRKAAS LTEDRDRGRD AVKREAALPP VSPLKAALSE EELEKKSKAI IEEYLHLNDM 

      1270       1280       1290       1300       1310       1320 
KEAVQCVQEL ASPSLLFIFV RHGVESTLER SAIAREHMGQ LLHQLLCAGH LSTAQYYQGL 

      1330       1340       1350       1360       1370       1380 
YEILELAEDM EIDIPHVWLY LAELVTPILQ EGGVPMGELF REITKPLRPL GKAASLLLEI 

      1390       1400       1410       1420       1430       1440 
LGLLCKSMGP KKVGTLWREA GLSWKEFLPE GQDIGAFVAE QKVEYTLGEE SEAPGQRALP 

      1450       1460       1470       1480       1490       1500 
SEELNRQLEK LLKEGSSNQR VFDWIEANLS EQQIVSNTLV RALMTAVCYS AIIFETPLRV 

      1510       1520       1530       1540       1550       1560 
DVAVLKARAK LLQKYLCDEQ KELQALYALQ ALVVTLEQPP NLLRMFFDAL YDEDVVKEDA 

      1570       1580       1590       1600 
FYSWESSKDP AEQQGKGVAL KSVTAFFKWL REAEEESDHN

Q04637 in FASTA format

View entry in raw text format (no links)
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	BLAST submission on ExPASy/SIB or at NCBI (USA)		Sequence analysis tools: ProtParam, ProtScale, Compute pI/Mw, PeptideMass, PeptideCutter, Dotlet (Java)
	ScanProsite, MotifScan		Submit a homology modeling request to SWISS-MODEL
	NPSA Sequence analysis tools