IF4G2_HUMAN
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 03-AUG-2022, entry version 201.
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}, and
RC 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 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 [15]
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 [16]
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 [17]
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 [18]
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 [19]
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 [20]
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 [21]
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 [22]
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 [23]
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 [24]
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 [25]
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 [26]
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. Binds EIF4A and EIF3. Interacts with MIF4GD.
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};
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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; 174.
DR DIP; DIP-31366N; -.
DR IntAct; P78344; 47.
DR MINT; P78344; -.
DR STRING; 9606.ENSP00000433664; -.
DR GlyGen; P78344; 1 site, 1 O-linked glycan (1 site).
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; P78344; -.
DR PeptideAtlas; P78344; -.
DR PRIDE; P78344; -.
DR ProteomicsDB; 57574; -. [P78344-1]
DR ProteomicsDB; 57575; -. [P78344-2]
DR Antibodypedia; 1569; 459 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 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; SRIMHEC; -.
DR OrthoDB; 594395at2759; -.
DR PhylomeDB; P78344; -.
DR PathwayCommons; P78344; -.
DR Reactome; R-HSA-1169408; ISG15 antiviral mechanism.
DR SignaLink; P78344; -.
DR SIGNOR; P78344; -.
DR BioGRID-ORCS; 1982; 513 hits in 1021 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 208 other tissues.
DR ExpressionAtlas; P78344; baseline and differential.
DR Genevisible; P78344; HS.
DR GO; GO:0005912; C:adherens junction; HDA:BHF-UCL.
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:0034645; P:cellular macromolecule biosynthetic process; IGI:ParkinsonsUK-UCL.
DR GO; GO:0010507; P:negative regulation of autophagy; IMP:ParkinsonsUK-UCL.
DR GO; GO:0030307; P:positive regulation of cell growth; IMP:ParkinsonsUK-UCL.
DR GO; GO:0051726; P:regulation of cell cycle; TAS:ProtInc.
DR GO; GO:0006446; P:regulation of translational initiation; IDA:UniProtKB.
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; PTHR23253; 1.
DR Pfam; PF02847; MA3; 1.
DR Pfam; PF02854; MIF4G; 1.
DR Pfam; PF02020; W2; 1.
DR SMART; SM00515; eIF5C; 1.
DR SMART; SM00544; MA3; 1.
DR SMART; SM00543; MIF4G; 1.
DR SUPFAM; SSF48371; SSF48371; 3.
DR PROSITE; PS51366; MI; 1.
DR PROSITE; PS51363; W2; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Acetylation; Alternative 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
