ID IF4G2_HUMAN Reviewed; 907 AA. AC P78344; O60877; P78404; Q0VH00; Q0VH01; Q2NKW9; Q49A79; Q53EU1; Q58EZ2; AC Q8NI71; Q96C16; DT 30-APR-2003, integrated into UniProtKB/Swiss-Prot. DT 01-MAY-1997, sequence version 1. DT 27-MAR-2024, entry version 210. DE RecName: Full=Eukaryotic translation initiation factor 4 gamma 2; DE Short=eIF-4-gamma 2; DE Short=eIF-4G 2; DE Short=eIF4G 2; DE AltName: Full=Death-associated protein 5; DE Short=DAP-5; DE AltName: Full=p97; GN Name=EIF4G2 {ECO:0000312|HGNC:HGNC:3297}; GN Synonyms=DAP5 {ECO:0000303|PubMed:9032289}; ORFNames=OK/SW-cl.75; OS Homo sapiens (Human). OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia; OC Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini; Hominidae; OC Homo. OX NCBI_TaxID=9606; RN [1] {ECO:0000305} RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), FUNCTION, TISSUE SPECIFICITY, RP IDENTIFICATION OF A NON-AUG INITIATOR START CODON, AND INTERACTION WITH RP EIF4A AND EIF3. RC TISSUE=Placenta {ECO:0000269|PubMed:9049310}; RX PubMed=9049310; DOI=10.1093/emboj/16.4.817; RA Imataka H., Olsen H.S., Sonenberg N.; RT "A new translational regulator with homology to eukaryotic translation RT initiation factor 4G."; RL EMBO J. 16:817-825(1997). RN [2] {ECO:0000305} RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), TISSUE SPECIFICITY, AND INTERACTION RP WITH EIF4A. RC TISSUE=Liver {ECO:0000269|PubMed:9030685}; RX PubMed=9030685; DOI=10.1101/gad.11.3.321; RA Yamanaka S., Poksay K.S., Arnold K.S., Innerarity T.L.; RT "A novel translational repressor mRNA is edited extensively in livers RT containing tumors caused by the transgene expression of the apoB mRNA- RT editing enzyme."; RL Genes Dev. 11:321-333(1997). RN [3] {ECO:0000305} RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), FUNCTION, AND TISSUE SPECIFICITY. RC TISSUE=Kidney {ECO:0000269|PubMed:9032289}; RX PubMed=9032289; DOI=10.1128/mcb.17.3.1615; RA Levy-Strumpf N., Deiss L.P., Berissi H., Kimchi A.; RT "DAP-5, a novel homolog of eukaryotic translation initiation factor 4G RT isolated as a putative modulator of gamma interferon-induced programmed RT cell death."; RL Mol. Cell. Biol. 17:1615-1625(1997). RN [4] {ECO:0000305} RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1). RC TISSUE=Kidney; RA Totoki Y., Toyoda A., Takeda T., Sakaki Y., Tanaka A., Yokoyama S.; RL Submitted (APR-2005) to the EMBL/GenBank/DDBJ databases. RN [5] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RX PubMed=16554811; DOI=10.1038/nature04632; RA Taylor T.D., Noguchi H., Totoki Y., Toyoda A., Kuroki Y., Dewar K., RA Lloyd C., Itoh T., Takeda T., Kim D.-W., She X., Barlow K.F., Bloom T., RA Bruford E., Chang J.L., Cuomo C.A., Eichler E., FitzGerald M.G., RA Jaffe D.B., LaButti K., Nicol R., Park H.-S., Seaman C., Sougnez C., RA Yang X., Zimmer A.R., Zody M.C., Birren B.W., Nusbaum C., Fujiyama A., RA Hattori M., Rogers J., Lander E.S., Sakaki Y.; RT "Human chromosome 11 DNA sequence and analysis including novel gene RT identification."; RL Nature 440:497-500(2006). RN [6] {ECO:0000305} RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 1 AND 2). RC TISSUE=Retinal pigment epithelium, Skin {ECO:0000269|PubMed:15489334}, RC and Testis {ECO:0000269|PubMed:15489334}; RX PubMed=15489334; DOI=10.1101/gr.2596504; RG The MGC Project Team; RT "The status, quality, and expansion of the NIH full-length cDNA project: RT the Mammalian Gene Collection (MGC)."; RL Genome Res. 14:2121-2127(2004). RN [7] {ECO:0000305} RP PROTEIN SEQUENCE OF 1-12, AND ACETYLATION AT MET-1. RC TISSUE=Platelet {ECO:0000269|PubMed:12665801}; RX PubMed=12665801; DOI=10.1038/nbt810; RA Gevaert K., Goethals M., Martens L., Van Damme J., Staes A., Thomas G.R., RA Vandekerckhove J.; RT "Exploring proteomes and analyzing protein processing by mass spectrometric RT identification of sorted N-terminal peptides."; RL Nat. Biotechnol. 21:566-569(2003). RN [8] {ECO:0000305} RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 679-907. RC TISSUE=Colon adenocarcinoma {ECO:0000269|Ref.8}; RA Shichijo S., Itoh K.; RT "Identification of immuno-peptidmics that are recognized by tumor-reactive RT CTL generated from TIL of colon cancer patients."; RL Submitted (JUN-2001) to the EMBL/GenBank/DDBJ databases. RN [9] {ECO:0000305} RP INTERACTION WITH MKNK1. RX PubMed=9878069; DOI=10.1093/emboj/18.1.270; RA Pyronnet S., Imataka H., Gingras A.-C., Fukunaga R., Hunter T., RA Sonenberg N.; RT "Human eukaryotic translation initiation factor 4G (eIF4G) recruits mnk1 to RT phosphorylate eIF4E."; RL EMBO J. 18:270-279(1999). RN [10] {ECO:0000305} RP FUNCTION, AND PHOSPHORYLATION. RX PubMed=11511540; DOI=10.1101/gad.889201; RA Pyronnet S., Dostie J., Sonenberg N.; RT "Suppression of cap-dependent translation in mitosis."; RL Genes Dev. 15:2083-2093(2001). RN [11] {ECO:0000305} RP FUNCTION. RX PubMed=11943866; DOI=10.1073/pnas.082102499; RA Henis-Korenblit S., Shani G., Sines T., Marash L., Shohat G., Kimchi A.; RT "The caspase-cleaved DAP5 protein supports internal ribosome entry site- RT mediated translation of death proteins."; RL Proc. Natl. Acad. Sci. U.S.A. 99:5400-5405(2002). RN [12] RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS]. RC TISSUE=Cervix carcinoma; RX PubMed=16964243; DOI=10.1038/nbt1240; RA Beausoleil S.A., Villen J., Gerber S.A., Rush J., Gygi S.P.; RT "A probability-based approach for high-throughput protein phosphorylation RT analysis and site localization."; RL Nat. Biotechnol. 24:1285-1292(2006). RN [13] RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS]. RC TISSUE=Platelet; RX PubMed=18088087; DOI=10.1021/pr0704130; RA Zahedi R.P., Lewandrowski U., Wiesner J., Wortelkamp S., Moebius J., RA Schuetz C., Walter U., Gambaryan S., Sickmann A.; RT "Phosphoproteome of resting human platelets."; RL J. Proteome Res. 7:526-534(2008). RN [14] RP INTERACTION WITH DAZAP2. RX PubMed=17984221; DOI=10.1128/mcb.01226-07; RA Kim J.E., Ryu I., Kim W.J., Song O.K., Ryu J., Kwon M.Y., Kim J.H., RA Jang S.K.; RT "Proline-rich transcript in brain protein induces stress granule RT formation."; RL Mol. Cell. Biol. 28:803-813(2008). RN [15] RP INTERACTION WITH MIF4GD. RX PubMed=18025107; DOI=10.1128/mcb.01500-07; RA Cakmakci N.G., Lerner R.S., Wagner E.J., Zheng L., Marzluff W.F.; RT "SLIP1, a factor required for activation of histone mRNA translation by the RT stem-loop binding protein."; RL Mol. Cell. Biol. 28:1182-1194(2008). RN [16] RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-514, AND IDENTIFICATION BY RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS]. RC TISSUE=Cervix carcinoma; RX PubMed=18669648; DOI=10.1073/pnas.0805139105; RA Dephoure N., Zhou C., Villen J., Beausoleil S.A., Bakalarski C.E., RA Elledge S.J., Gygi S.P.; RT "A quantitative atlas of mitotic phosphorylation."; RL Proc. Natl. Acad. Sci. U.S.A. 105:10762-10767(2008). RN [17] RP ACETYLATION [LARGE SCALE ANALYSIS] AT MET-1, AND IDENTIFICATION BY MASS RP SPECTROMETRY [LARGE SCALE ANALYSIS]. RX PubMed=19413330; DOI=10.1021/ac9004309; RA Gauci S., Helbig A.O., Slijper M., Krijgsveld J., Heck A.J., Mohammed S.; RT "Lys-N and trypsin cover complementary parts of the phosphoproteome in a RT refined SCX-based approach."; RL Anal. Chem. 81:4493-4501(2009). RN [18] RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-508, AND IDENTIFICATION BY RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS]. RC TISSUE=Leukemic T-cell; RX PubMed=19690332; DOI=10.1126/scisignal.2000007; RA Mayya V., Lundgren D.H., Hwang S.-I., Rezaul K., Wu L., Eng J.K., RA Rodionov V., Han D.K.; RT "Quantitative phosphoproteomic analysis of T cell receptor signaling RT reveals system-wide modulation of protein-protein interactions."; RL Sci. Signal. 2:RA46-RA46(2009). RN [19] RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-395 AND SER-902, AND RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS]. RC TISSUE=Cervix carcinoma; RX PubMed=20068231; DOI=10.1126/scisignal.2000475; RA Olsen J.V., Vermeulen M., Santamaria A., Kumar C., Miller M.L., RA Jensen L.J., Gnad F., Cox J., Jensen T.S., Nigg E.A., Brunak S., Mann M.; RT "Quantitative phosphoproteomics reveals widespread full phosphorylation RT site occupancy during mitosis."; RL Sci. Signal. 3:RA3-RA3(2010). RN [20] RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS]. RX PubMed=21269460; DOI=10.1186/1752-0509-5-17; RA Burkard T.R., Planyavsky M., Kaupe I., Breitwieser F.P., Buerckstuemmer T., RA Bennett K.L., Superti-Furga G., Colinge J.; RT "Initial characterization of the human central proteome."; RL BMC Syst. Biol. 5:17-17(2011). RN [21] RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-902, AND IDENTIFICATION BY RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS]. RX PubMed=21406692; DOI=10.1126/scisignal.2001570; RA Rigbolt K.T., Prokhorova T.A., Akimov V., Henningsen J., Johansen P.T., RA Kratchmarova I., Kassem M., Mann M., Olsen J.V., Blagoev B.; RT "System-wide temporal characterization of the proteome and phosphoproteome RT of human embryonic stem cell differentiation."; RL Sci. Signal. 4:RS3-RS3(2011). RN [22] RP ACETYLATION [LARGE SCALE ANALYSIS] AT MET-1, AND IDENTIFICATION BY MASS RP SPECTROMETRY [LARGE SCALE ANALYSIS]. RX PubMed=22223895; DOI=10.1074/mcp.m111.015131; RA Bienvenut W.V., Sumpton D., Martinez A., Lilla S., Espagne C., Meinnel T., RA Giglione C.; RT "Comparative large-scale characterisation of plant vs. mammal proteins RT reveals similar and idiosyncratic N-alpha acetylation features."; RL Mol. Cell. Proteomics 11:M111.015131-M111.015131(2012). RN [23] RP ACETYLATION [LARGE SCALE ANALYSIS] AT MET-1, AND IDENTIFICATION BY MASS RP SPECTROMETRY [LARGE SCALE ANALYSIS]. RX PubMed=22814378; DOI=10.1073/pnas.1210303109; RA Van Damme P., Lasa M., Polevoda B., Gazquez C., Elosegui-Artola A., RA Kim D.S., De Juan-Pardo E., Demeyer K., Hole K., Larrea E., Timmerman E., RA Prieto J., Arnesen T., Sherman F., Gevaert K., Aldabe R.; RT "N-terminal acetylome analyses and functional insights of the N-terminal RT acetyltransferase NatB."; RL Proc. Natl. Acad. Sci. U.S.A. 109:12449-12454(2012). RN [24] RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-11; THR-89; SER-443 AND RP THR-508, AND IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS]. RC TISSUE=Cervix carcinoma, and Erythroleukemia; RX PubMed=23186163; DOI=10.1021/pr300630k; RA Zhou H., Di Palma S., Preisinger C., Peng M., Polat A.N., Heck A.J., RA Mohammed S.; RT "Toward a comprehensive characterization of a human cancer cell RT phosphoproteome."; RL J. Proteome Res. 12:260-271(2013). RN [25] RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-508, AND IDENTIFICATION BY RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS]. RC TISSUE=Liver; RX PubMed=24275569; DOI=10.1016/j.jprot.2013.11.014; RA Bian Y., Song C., Cheng K., Dong M., Wang F., Huang J., Sun D., Wang L., RA Ye M., Zou H.; RT "An enzyme assisted RP-RPLC approach for in-depth analysis of human liver RT phosphoproteome."; RL J. Proteomics 96:253-262(2014). RN [26] RP METHYLATION [LARGE SCALE ANALYSIS] AT ARG-360; LYS-431 AND ARG-505, AND RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS]. RC TISSUE=Colon carcinoma; RX PubMed=24129315; DOI=10.1074/mcp.o113.027870; RA Guo A., Gu H., Zhou J., Mulhern D., Wang Y., Lee K.A., Yang V., Aguiar M., RA Kornhauser J., Jia X., Ren J., Beausoleil S.A., Silva J.C., Vemulapalli V., RA Bedford M.T., Comb M.J.; RT "Immunoaffinity enrichment and mass spectrometry analysis of protein RT methylation."; RL Mol. Cell. Proteomics 13:372-387(2014). RN [27] RP SUMOYLATION [LARGE SCALE ANALYSIS] AT LYS-575, AND IDENTIFICATION BY MASS RP SPECTROMETRY [LARGE SCALE ANALYSIS]. RX PubMed=28112733; DOI=10.1038/nsmb.3366; RA Hendriks I.A., Lyon D., Young C., Jensen L.J., Vertegaal A.C., RA Nielsen M.L.; RT "Site-specific mapping of the human SUMO proteome reveals co-modification RT with phosphorylation."; RL Nat. Struct. Mol. Biol. 24:325-336(2017). CC -!- FUNCTION: Appears to play a role in the switch from cap-dependent to CC IRES-mediated translation during mitosis, apoptosis and viral CC infection. Cleaved by some caspases and viral proteases. CC {ECO:0000269|PubMed:11511540, ECO:0000269|PubMed:11943866, CC ECO:0000269|PubMed:9032289, ECO:0000269|PubMed:9049310}. CC -!- SUBUNIT: Interacts with the serine/threonine protein kinases MKNK1 and CC MKNK2 (PubMed:9878069). Binds EIF4A and EIF3 (PubMed:9049310, CC PubMed:9030685). Interacts with MIF4GD (PubMed:18025107). Interacts CC with DAZAP2 (PubMed:17984221). {ECO:0000269|PubMed:17984221, CC ECO:0000269|PubMed:18025107, ECO:0000269|PubMed:9030685, CC ECO:0000269|PubMed:9049310, ECO:0000269|PubMed:9878069}. CC -!- INTERACTION: CC P78344; P20042: EIF2S2; NbExp=4; IntAct=EBI-296519, EBI-711977; CC P78344; P60842: EIF4A1; NbExp=3; IntAct=EBI-296519, EBI-73449; CC P78344; P04792: HSPB1; NbExp=3; IntAct=EBI-296519, EBI-352682; CC P78344; PRO_0000308465 [P29991]; Xeno; NbExp=4; IntAct=EBI-296519, EBI-8826747; CC P78344-1; P60842: EIF4A1; NbExp=3; IntAct=EBI-16040248, EBI-73449; CC -!- ALTERNATIVE PRODUCTS: CC Event=Alternative splicing; Named isoforms=2; CC Name=1; CC IsoId=P78344-1; Sequence=Displayed; CC Name=2; CC IsoId=P78344-2; Sequence=VSP_038726; CC -!- TISSUE SPECIFICITY: Ubiquitously expressed in all adult tissues CC examined, with high levels in skeletal muscle and heart. Also expressed CC in fetal brain, lung, liver and kidney. {ECO:0000269|PubMed:9030685, CC ECO:0000269|PubMed:9032289, ECO:0000269|PubMed:9049310}. CC -!- PTM: Phosphorylation; hyperphosphorylated during mitosis. CC {ECO:0000269|PubMed:11511540}. CC -!- MISCELLANEOUS: This gene has been shown to be extensively edited in the CC liver of APOBEC1 transgenic animal model. Its aberrant editing could CC contribute to the potent oncogenesis induced by overexpression of CC APOBEC1. The aberrant edited sequence, called NAT1, is likely to be a CC fundamental translational repressor. CC -!- SIMILARITY: Belongs to the eukaryotic initiation factor 4G family. CC {ECO:0000305}. CC -!- CAUTION: According to PubMed:9049310, this sequence initiates CC exclusively at a GTG codon. {ECO:0000305}. CC -!- SEQUENCE CAUTION: CC Sequence=BAB93515.1; Type=Erroneous initiation; Note=Truncated N-terminus.; Evidence={ECO:0000305}; CC Sequence=BAD97268.1; Type=Miscellaneous discrepancy; Note=Unusual initiator. The initiator methionine is coded by a non-canonical GTG valine codon.; Evidence={ECO:0000305}; CC Sequence=CAA61857.1; Type=Miscellaneous discrepancy; Note=Unusual initiator. The initiator methionine is coded by a non-canonical GTG valine codon.; Evidence={ECO:0000305}; CC --------------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution (CC BY 4.0) License CC --------------------------------------------------------------------------- DR EMBL; U73824; AAB49973.1; -; mRNA. DR EMBL; U76111; AAC51166.1; -; mRNA. DR EMBL; X89713; CAA61857.1; ALT_SEQ; mRNA. DR EMBL; AK223548; BAD97268.1; ALT_SEQ; mRNA. DR EMBL; AC116535; -; NOT_ANNOTATED_CDS; Genomic_DNA. DR EMBL; BC014930; AAH14930.2; -; mRNA. DR EMBL; BC018746; AAH18746.1; -; mRNA. DR EMBL; BC018975; AAH18975.1; -; mRNA. DR EMBL; BC039851; AAH39851.1; -; mRNA. DR EMBL; BC043149; AAH43149.2; -; mRNA. DR EMBL; BC111415; AAI11416.1; -; mRNA. DR EMBL; BC111548; AAI11549.2; -; mRNA. DR EMBL; AB063323; BAB93515.1; ALT_INIT; mRNA. DR CCDS; CCDS31428.1; -. [P78344-1] DR CCDS; CCDS41618.1; -. [P78344-2] DR RefSeq; NP_001036024.3; NM_001042559.2. [P78344-2] DR RefSeq; NP_001166176.1; NM_001172705.1. [P78344-1] DR RefSeq; NP_001409.3; NM_001418.3. [P78344-1] DR PDB; 3D3M; X-ray; 1.90 A; A/B=730-897. DR PDB; 3L6A; X-ray; 2.00 A; A=540-897. DR PDB; 4IUL; X-ray; 2.30 A; A/B=61-323. DR PDBsum; 3D3M; -. DR PDBsum; 3L6A; -. DR PDBsum; 4IUL; -. DR AlphaFoldDB; P78344; -. DR SMR; P78344; -. DR BioGRID; 108297; 204. DR DIP; DIP-31366N; -. DR IntAct; P78344; 51. DR MINT; P78344; -. DR STRING; 9606.ENSP00000433664; -. DR GlyCosmos; P78344; 1 site, 1 glycan. DR GlyGen; P78344; 2 sites, 1 O-linked glycan (2 sites). DR iPTMnet; P78344; -. DR MetOSite; P78344; -. DR PhosphoSitePlus; P78344; -. DR SwissPalm; P78344; -. DR BioMuta; EIF4G2; -. DR DMDM; 30315906; -. DR EPD; P78344; -. DR jPOST; P78344; -. DR MassIVE; P78344; -. DR MaxQB; P78344; -. DR PaxDb; 9606-ENSP00000433664; -. DR PeptideAtlas; P78344; -. DR ProteomicsDB; 57574; -. [P78344-1] DR ProteomicsDB; 57575; -. [P78344-2] DR Pumba; P78344; -. DR Antibodypedia; 1569; 503 antibodies from 40 providers. DR DNASU; 1982; -. DR Ensembl; ENST00000339995.11; ENSP00000340281.6; ENSG00000110321.19. [P78344-1] DR Ensembl; ENST00000396525.7; ENSP00000379778.3; ENSG00000110321.19. [P78344-2] DR Ensembl; ENST00000525681.6; ENSP00000433371.2; ENSG00000110321.19. [P78344-1] DR Ensembl; ENST00000526148.6; ENSP00000433664.2; ENSG00000110321.19. [P78344-1] DR GeneID; 1982; -. DR KEGG; hsa:1982; -. DR MANE-Select; ENST00000339995.11; ENSP00000340281.6; NM_001418.4; NP_001409.3. DR UCSC; uc057zbi.1; human. [P78344-1] DR AGR; HGNC:3297; -. DR CTD; 1982; -. DR DisGeNET; 1982; -. DR GeneCards; EIF4G2; -. DR HGNC; HGNC:3297; EIF4G2. DR HPA; ENSG00000110321; Low tissue specificity. DR MIM; 602325; gene. DR neXtProt; NX_P78344; -. DR OpenTargets; ENSG00000110321; -. DR PharmGKB; PA27723; -. DR VEuPathDB; HostDB:ENSG00000110321; -. DR eggNOG; KOG0401; Eukaryota. DR GeneTree; ENSGT00940000154675; -. DR InParanoid; P78344; -. DR OMA; CAPLDIN; -. DR OrthoDB; 92033at2759; -. DR PhylomeDB; P78344; -. DR PathwayCommons; P78344; -. DR Reactome; R-HSA-1169408; ISG15 antiviral mechanism. DR SignaLink; P78344; -. DR SIGNOR; P78344; -. DR BioGRID-ORCS; 1982; 519 hits in 1085 CRISPR screens. DR ChiTaRS; EIF4G2; human. DR EvolutionaryTrace; P78344; -. DR GeneWiki; EIF4G2; -. DR GenomeRNAi; 1982; -. DR Pharos; P78344; Tbio. DR PRO; PR:P78344; -. DR Proteomes; UP000005640; Chromosome 11. DR RNAct; P78344; Protein. DR Bgee; ENSG00000110321; Expressed in visceral pleura and 210 other cell types or tissues. DR ExpressionAtlas; P78344; baseline and differential. DR GO; GO:0005912; C:adherens junction; HDA:BHF-UCL. DR GO; GO:0030424; C:axon; IEA:Ensembl. DR GO; GO:0005829; C:cytosol; IDA:HPA. DR GO; GO:0016281; C:eukaryotic translation initiation factor 4F complex; IDA:UniProtKB. DR GO; GO:0016020; C:membrane; HDA:UniProtKB. DR GO; GO:0045296; F:cadherin binding; HDA:BHF-UCL. DR GO; GO:0003729; F:mRNA binding; IBA:GO_Central. DR GO; GO:0003723; F:RNA binding; HDA:UniProtKB. DR GO; GO:0008135; F:translation factor activity, RNA binding; IDA:UniProtKB. DR GO; GO:0003743; F:translation initiation factor activity; IDA:UniProtKB. DR GO; GO:0008219; P:cell death; TAS:ProtInc. DR GO; GO:0007507; P:heart development; IEA:Ensembl. DR GO; GO:0009059; P:macromolecule biosynthetic process; IGI:ParkinsonsUK-UCL. DR GO; GO:0010507; P:negative regulation of autophagy; IMP:ParkinsonsUK-UCL. DR GO; GO:0045773; P:positive regulation of axon extension; IEA:Ensembl. DR GO; GO:0030307; P:positive regulation of cell growth; IMP:ParkinsonsUK-UCL. DR GO; GO:0060999; P:positive regulation of dendritic spine development; IEA:Ensembl. DR GO; GO:0045727; P:positive regulation of translation; IEA:Ensembl. DR GO; GO:0051726; P:regulation of cell cycle; TAS:ProtInc. DR GO; GO:0006446; P:regulation of translational initiation; IDA:UniProtKB. DR CDD; cd11559; W2_eIF4G1_like; 1. DR Gene3D; 1.25.40.180; -; 3. DR InterPro; IPR016024; ARM-type_fold. DR InterPro; IPR045208; IF4G. DR InterPro; IPR003891; Initiation_fac_eIF4g_MI. DR InterPro; IPR003890; MIF4G-like_typ-3. DR InterPro; IPR003307; W2_domain. DR PANTHER; PTHR23253; EUKARYOTIC TRANSLATION INITIATION FACTOR 4 GAMMA; 1. DR PANTHER; PTHR23253:SF82; EUKARYOTIC TRANSLATION INITIATION FACTOR 4 GAMMA 2; 1. DR Pfam; PF02847; MA3; 1. DR Pfam; PF02854; MIF4G; 1. DR Pfam; PF02020; W2; 1. DR SMART; SM00515; eIF5C; 1. DR SMART; SM00544; MA3; 1. DR SMART; SM00543; MIF4G; 1. DR SUPFAM; SSF48371; ARM repeat; 3. DR PROSITE; PS51366; MI; 1. DR PROSITE; PS51363; W2; 1. DR Genevisible; P78344; HS. PE 1: Evidence at protein level; KW 3D-structure; Acetylation; Alternative splicing; Direct protein sequencing; KW Initiation factor; Isopeptide bond; Methylation; Phosphoprotein; KW Protein biosynthesis; Reference proteome; Repressor; KW Translation regulation; Ubl conjugation. FT CHAIN 1..907 FT /note="Eukaryotic translation initiation factor 4 gamma 2" FT /id="PRO_0000213325" FT DOMAIN 78..308 FT /note="MIF4G" FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00698" FT DOMAIN 543..666 FT /note="MI" FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00698" FT DOMAIN 720..904 FT /note="W2" FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00695" FT REGION 1..71 FT /note="Disordered" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT REGION 498..541 FT /note="Disordered" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT COMPBIAS 38..63 FT /note="Polar residues" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT MOD_RES 1 FT /note="N-acetylmethionine" FT /evidence="ECO:0000269|PubMed:12665801, FT ECO:0007744|PubMed:19413330, ECO:0007744|PubMed:22223895, FT ECO:0007744|PubMed:22814378" FT MOD_RES 11 FT /note="Phosphoserine" FT /evidence="ECO:0007744|PubMed:23186163" FT MOD_RES 89 FT /note="Phosphothreonine" FT /evidence="ECO:0007744|PubMed:23186163" FT MOD_RES 360 FT /note="Omega-N-methylarginine" FT /evidence="ECO:0007744|PubMed:24129315" FT MOD_RES 395 FT /note="Phosphoserine" FT /evidence="ECO:0007744|PubMed:20068231" FT MOD_RES 431 FT /note="N6-methyllysine" FT /evidence="ECO:0007744|PubMed:24129315" FT MOD_RES 443 FT /note="Phosphoserine" FT /evidence="ECO:0007744|PubMed:23186163" FT MOD_RES 505 FT /note="Omega-N-methylarginine" FT /evidence="ECO:0007744|PubMed:24129315" FT MOD_RES 508 FT /note="Phosphothreonine" FT /evidence="ECO:0007744|PubMed:19690332, FT ECO:0007744|PubMed:23186163, ECO:0007744|PubMed:24275569" FT MOD_RES 514 FT /note="Phosphothreonine" FT /evidence="ECO:0007744|PubMed:18669648" FT MOD_RES 902 FT /note="Phosphoserine" FT /evidence="ECO:0007744|PubMed:20068231, FT ECO:0007744|PubMed:21406692" FT CROSSLNK 575 FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with FT G-Cter in SUMO2)" FT /evidence="ECO:0007744|PubMed:28112733" FT VAR_SEQ 434..471 FT /note="Missing (in isoform 2)" FT /evidence="ECO:0000303|PubMed:15489334" FT /id="VSP_038726" FT VARIANT 236 FT /note="L -> M (in dbSNP:rs34885591)" FT /id="VAR_048923" FT CONFLICT 169 FT /note="S -> P (in Ref. 2; AAC51166)" FT /evidence="ECO:0000305" FT CONFLICT 233 FT /note="K -> Q (in Ref. 2; AAC51166)" FT /evidence="ECO:0000305" FT CONFLICT 245 FT /note="K -> Q (in Ref. 2; AAC51166)" FT /evidence="ECO:0000305" FT CONFLICT 351 FT /note="F -> L (in Ref. 2; AAC51166)" FT /evidence="ECO:0000305" FT CONFLICT 441 FT /note="N -> S (in Ref. 6; AAH18746)" FT /evidence="ECO:0000305" FT CONFLICT 531 FT /note="A -> G (in Ref. 2; AAC51166)" FT /evidence="ECO:0000305" FT CONFLICT 534 FT /note="S -> N (in Ref. 6; AAH43149)" FT /evidence="ECO:0000305" FT CONFLICT 613 FT /note="A -> G (in Ref. 2; AAC51166)" FT /evidence="ECO:0000305" FT CONFLICT 861 FT /note="I -> S (in Ref. 2; AAC51166)" FT /evidence="ECO:0000305" FT CONFLICT 899 FT /note="E -> G (in Ref. 2; AAC51166)" FT /evidence="ECO:0000305" FT HELIX 68..86 FT /evidence="ECO:0007829|PDB:4IUL" FT TURN 90..92 FT /evidence="ECO:0007829|PDB:4IUL" FT HELIX 93..103 FT /evidence="ECO:0007829|PDB:4IUL" FT HELIX 108..124 FT /evidence="ECO:0007829|PDB:4IUL" FT HELIX 126..128 FT /evidence="ECO:0007829|PDB:4IUL" FT HELIX 129..142 FT /evidence="ECO:0007829|PDB:4IUL" FT TURN 149..152 FT /evidence="ECO:0007829|PDB:4IUL" FT HELIX 162..182 FT /evidence="ECO:0007829|PDB:4IUL" FT STRAND 188..190 FT /evidence="ECO:0007829|PDB:4IUL" FT HELIX 196..218 FT /evidence="ECO:0007829|PDB:4IUL" FT TURN 219..221 FT /evidence="ECO:0007829|PDB:4IUL" FT HELIX 225..236 FT /evidence="ECO:0007829|PDB:4IUL" FT STRAND 240..242 FT /evidence="ECO:0007829|PDB:4IUL" FT HELIX 244..246 FT /evidence="ECO:0007829|PDB:4IUL" FT HELIX 248..265 FT /evidence="ECO:0007829|PDB:4IUL" FT HELIX 268..270 FT /evidence="ECO:0007829|PDB:4IUL" FT HELIX 271..282 FT /evidence="ECO:0007829|PDB:4IUL" FT TURN 283..286 FT /evidence="ECO:0007829|PDB:4IUL" FT HELIX 292..306 FT /evidence="ECO:0007829|PDB:4IUL" FT TURN 307..309 FT /evidence="ECO:0007829|PDB:4IUL" FT HELIX 541..558 FT /evidence="ECO:0007829|PDB:3L6A" FT HELIX 561..571 FT /evidence="ECO:0007829|PDB:3L6A" FT HELIX 575..577 FT /evidence="ECO:0007829|PDB:3L6A" FT HELIX 578..590 FT /evidence="ECO:0007829|PDB:3L6A" FT HELIX 594..609 FT /evidence="ECO:0007829|PDB:3L6A" FT HELIX 615..627 FT /evidence="ECO:0007829|PDB:3L6A" FT HELIX 629..635 FT /evidence="ECO:0007829|PDB:3L6A" FT HELIX 639..652 FT /evidence="ECO:0007829|PDB:3L6A" FT HELIX 658..665 FT /evidence="ECO:0007829|PDB:3L6A" FT HELIX 666..668 FT /evidence="ECO:0007829|PDB:3L6A" FT TURN 669..672 FT /evidence="ECO:0007829|PDB:3L6A" FT HELIX 673..684 FT /evidence="ECO:0007829|PDB:3L6A" FT HELIX 687..697 FT /evidence="ECO:0007829|PDB:3L6A" FT HELIX 702..704 FT /evidence="ECO:0007829|PDB:3L6A" FT HELIX 707..709 FT /evidence="ECO:0007829|PDB:3L6A" FT HELIX 712..722 FT /evidence="ECO:0007829|PDB:3L6A" FT HELIX 725..727 FT /evidence="ECO:0007829|PDB:3L6A" FT HELIX 731..743 FT /evidence="ECO:0007829|PDB:3D3M" FT HELIX 747..757 FT /evidence="ECO:0007829|PDB:3D3M" FT HELIX 760..764 FT /evidence="ECO:0007829|PDB:3D3M" FT HELIX 766..784 FT /evidence="ECO:0007829|PDB:3D3M" FT HELIX 799..820 FT /evidence="ECO:0007829|PDB:3D3M" FT HELIX 824..840 FT /evidence="ECO:0007829|PDB:3D3M" FT HELIX 847..857 FT /evidence="ECO:0007829|PDB:3D3M" FT HELIX 863..871 FT /evidence="ECO:0007829|PDB:3D3M" FT HELIX 880..895 FT /evidence="ECO:0007829|PDB:3D3M" SQ SEQUENCE 907 AA; 102362 MW; 4EF050B5EEA4DF91 CRC64; MESAIAEGGA SRFSASSGGG GSRGAPQHYP KTAGNSEFLG KTPGQNAQKW IPARSTRRDD NSAANNSANE KERHDAIFRK VRGILNKLTP EKFDKLCLEL LNVGVESKLI LKGVILLIVD KALEEPKYSS LYAQLCLRLA EDAPNFDGPA AEGQPGQKQS TTFRRLLISK LQDEFENRTR NVDVYDKREN PLLPEEEEQR AIAKIKMLGN IKFIGELGKL DLIHESILHK CIKTLLEKKK RVQLKDMGED LECLCQIMRT VGPRLDHERA KSLMDQYFAR MCSLMLSKEL PARIRFLLQD TVELREHHWV PRKAFLDNGP KTINQIRQDA VKDLGVFIPA PMAQGMRSDF FLEGPFMPPR MKMDRDPLGG LADMFGQMPG SGIGTGPGVI QDRFSPTMGR HRSNQLFNGH GGHIMPPTQS QFGEMGGKFM KSQGLSQLYH NQSQGLLSQL QGQSKDMPPR FSKKGQLNAD EISLRPAQSF LMNKNQVPKL QPQITMIPPS AQPPRTQTPP LGQTPQLGLK TNPPLIQEKP AKTSKKPPPS KEELLKLTET VVTEYLNSGN ANEAVNGVRE MRAPKHFLPE MLSKVIILSL DRSDEDKEKA SSLISLLKQE GIATSDNFMQ AFLNVLDQCP KLEVDIPLVK SYLAQFAARA IISELVSISE LAQPLESGTH FPLFLLCLQQ LAKLQDREWL TELFQQSKVN MQKMLPEIDQ NKDRMLEILE GKGLSFLFPL LKLEKELLKQ IKLDPSPQTI YKWIKDNISP KLHVDKGFVN ILMTSFLQYI SSEVNPPSDE TDSSSAPSKE QLEQEKQLLL SFKPVMQKFL HDHVDLQVSA LYALQVHCYN SNFPKGMLLR FFVHFYDMEI IEEEAFLAWK EDITQEFPGK GKALFQVNQW LTWLETAEEE ESEEEAD //