IF4G1_MOUSE
ID IF4G1_MOUSE Reviewed; 1600 AA.
AC Q6NZJ6; Q6NZN8; Q8BW99;
DT 07-JUN-2005, integrated into UniProtKB/Swiss-Prot.
DT 05-JUL-2004, sequence version 1.
DT 03-AUG-2022, entry version 155.
DE RecName: Full=Eukaryotic translation initiation factor 4 gamma 1;
DE Short=eIF-4-gamma 1;
DE Short=eIF-4G 1;
DE Short=eIF-4G1;
GN Name=Eif4g1;
OS Mus musculus (Mouse).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae;
OC Murinae; Mus; Mus.
OX NCBI_TaxID=10090;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 1 AND 2).
RC STRAIN=C57BL/6J; TISSUE=Brain, and Fetal brain;
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 [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 1-520 (ISOFORM 2).
RC STRAIN=C57BL/6J; TISSUE=Lung;
RX PubMed=16141072; DOI=10.1126/science.1112014;
RA Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N.,
RA Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K.,
RA Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M., Davis M.J.,
RA Wilming L.G., Aidinis V., Allen J.E., Ambesi-Impiombato A., Apweiler R.,
RA Aturaliya R.N., Bailey T.L., Bansal M., Baxter L., Beisel K.W., Bersano T.,
RA Bono H., Chalk A.M., Chiu K.P., Choudhary V., Christoffels A.,
RA Clutterbuck D.R., Crowe M.L., Dalla E., Dalrymple B.P., de Bono B.,
RA Della Gatta G., di Bernardo D., Down T., Engstrom P., Fagiolini M.,
RA Faulkner G., Fletcher C.F., Fukushima T., Furuno M., Futaki S.,
RA Gariboldi M., Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E.,
RA Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N., Hill D.,
RA Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T., Jakt M.,
RA Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H., Kitano H.,
RA Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K., Kurochkin I.V.,
RA Lareau L.F., Lazarevic D., Lipovich L., Liu J., Liuni S., McWilliam S.,
RA Madan Babu M., Madera M., Marchionni L., Matsuda H., Matsuzawa S., Miki H.,
RA Mignone F., Miyake S., Morris K., Mottagui-Tabar S., Mulder N., Nakano N.,
RA Nakauchi H., Ng P., Nilsson R., Nishiguchi S., Nishikawa S., Nori F.,
RA Ohara O., Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G.,
RA Pesole G., Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z.,
RA Ringwald M., Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C.,
RA Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y.,
RA Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B., Sperling S.,
RA Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K., Tammoja K.,
RA Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A., Ueda H.R.,
RA van Nimwegen E., Verardo R., Wei C.L., Yagi K., Yamanishi H.,
RA Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C., Grimmond S.M.,
RA Teasdale R.D., Liu E.T., Brusic V., Quackenbush J., Wahlestedt C.,
RA Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y., Fukuda S.,
RA Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T., Iida J., Imamura K.,
RA Itoh M., Kato T., Kawaji H., Kawagashira N., Kawashima T., Kojima M.,
RA Kondo S., Konno H., Nakano K., Ninomiya N., Nishio T., Okada M., Plessy C.,
RA Shibata K., Shiraki T., Suzuki S., Tagami M., Waki K., Watahiki A.,
RA Okamura-Oho Y., Suzuki H., Kawai J., Hayashizaki Y.;
RT "The transcriptional landscape of the mammalian genome.";
RL Science 309:1559-1563(2005).
RN [3]
RP INTERACTION WITH EIF4E3.
RX PubMed=15153109; DOI=10.1111/j.1432-1033.2004.04149.x;
RA Joshi B., Cameron A., Jagus R.;
RT "Characterization of mammalian eIF4E-family members.";
RL Eur. J. Biochem. 271:2189-2203(2004).
RN [4]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-1231, AND IDENTIFICATION BY
RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Liver;
RX PubMed=17242355; DOI=10.1073/pnas.0609836104;
RA Villen J., Beausoleil S.A., Gerber S.A., Gygi S.P.;
RT "Large-scale phosphorylation analysis of mouse liver.";
RL Proc. Natl. Acad. Sci. U.S.A. 104:1488-1493(2007).
RN [5]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-1211, AND IDENTIFICATION BY
RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Liver;
RX PubMed=18630941; DOI=10.1021/pr800223m;
RA Zhou H., Ye M., Dong J., Han G., Jiang X., Wu R., Zou H.;
RT "Specific phosphopeptide enrichment with immobilized titanium ion affinity
RT chromatography adsorbent for phosphoproteome analysis.";
RL J. Proteome Res. 7:3957-3967(2008).
RN [6]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-1189 AND SER-1231, AND
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=19144319; DOI=10.1016/j.immuni.2008.11.006;
RA Trost M., English L., Lemieux S., Courcelles M., Desjardins M.,
RA Thibault P.;
RT "The phagosomal proteome in interferon-gamma-activated macrophages.";
RL Immunity 30:143-154(2009).
RN [7]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-1231 AND SER-1597, AND
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Embryonic fibroblast;
RX PubMed=19131326; DOI=10.1074/mcp.m800451-mcp200;
RA Sweet S.M., Bailey C.M., Cunningham D.L., Heath J.K., Cooper H.J.;
RT "Large scale localization of protein phosphorylation by use of electron
RT capture dissociation mass spectrometry.";
RL Mol. Cell. Proteomics 8:904-912(2009).
RN [8]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-15; THR-214; SER-230;
RP SER-1096 AND SER-1211, AND IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE
RP ANALYSIS].
RC TISSUE=Brain, Brown adipose tissue, Heart, Kidney, Liver, Lung, Pancreas,
RC Spleen, and Testis;
RX PubMed=21183079; DOI=10.1016/j.cell.2010.12.001;
RA Huttlin E.L., Jedrychowski M.P., Elias J.E., Goswami T., Rad R.,
RA Beausoleil S.A., Villen J., Haas W., Sowa M.E., Gygi S.P.;
RT "A tissue-specific atlas of mouse protein phosphorylation and expression.";
RL Cell 143:1174-1189(2010).
RN [9]
RP ACETYLATION [LARGE SCALE ANALYSIS] AT LYS-606, AND IDENTIFICATION BY MASS
RP SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Embryonic fibroblast;
RX PubMed=23806337; DOI=10.1016/j.molcel.2013.06.001;
RA Park J., Chen Y., Tishkoff D.X., Peng C., Tan M., Dai L., Xie Z., Zhang Y.,
RA Zwaans B.M., Skinner M.E., Lombard D.B., Zhao Y.;
RT "SIRT5-mediated lysine desuccinylation impacts diverse metabolic
RT pathways.";
RL Mol. Cell 50:919-930(2013).
RN [10]
RP METHYLATION [LARGE SCALE ANALYSIS] AT ARG-117; ARG-689; ARG-1036 AND
RP ARG-1046, AND IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Brain, and Embryo;
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).
CC -!- FUNCTION: Component of the protein complex eIF4F, which is involved in
CC the recognition of the mRNA cap, ATP-dependent unwinding of 5'-terminal
CC secondary structure and recruitment of mRNA to the ribosome. As a
CC member of the eIF4F complex, required for endoplasmic reticulum stress-
CC induced ATF4 mRNA translation (By similarity). {ECO:0000250,
CC ECO:0000250|UniProtKB:Q04637}.
CC -!- SUBUNIT: eIF4F is a multi-subunit complex, the composition of which
CC varies with external and internal environmental conditions. It is
CC composed of at least EIF4A, EIF4E and EIF4G1/EIF4G3. Interacts with
CC eIF3, mutually exclusive with EIF4A1 or EIFA2, EIF4E and through its N-
CC terminus with PAPBC1. Interacts through its C-terminus with the
CC serine/threonine kinases MKNK1, and with MKNK2. Appears to act as a
CC scaffold protein, holding these enzymes in place to phosphorylate
CC EIF4E. Non-phosphorylated EIF4EBP1 competes with EIF4G1/EIF4G3 to
CC interact with EIF4E; insulin stimulated MAP-kinase (MAPK1 and MAPK3)
CC phosphorylation of EIF4EBP1 causes dissociation of the complex allowing
CC EIF4G1/EIF4G3 to bind and consequent initiation of translation.
CC Interacts with CIRBP and MIF4GD. Interacts with RBM4. Interacts with
CC EIF4E3. Interacts with HNRNPD/AUF1; the interaction requires RNA.
CC Directly interacts with EIF4G1 in an RNA-independent manner (By
CC similarity). {ECO:0000250|UniProtKB:Q04637,
CC ECO:0000269|PubMed:15153109}.
CC -!- INTERACTION:
CC Q6NZJ6; Q8JZQ9: Eif3b; NbExp=2; IntAct=EBI-8175606, EBI-4286513;
CC Q6NZJ6; Q9QZD9: Eif3i; NbExp=3; IntAct=EBI-8175606, EBI-7466616;
CC Q6NZJ6; P60843: Eif4a1; NbExp=2; IntAct=EBI-8175606, EBI-6665935;
CC Q6NZJ6; P63073: Eif4e; NbExp=7; IntAct=EBI-8175606, EBI-2000006;
CC -!- SUBCELLULAR LOCATION: Cytoplasm, Stress granule
CC {ECO:0000250|UniProtKB:Q04637}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=2;
CC Name=1;
CC IsoId=Q6NZJ6-1; Sequence=Displayed;
CC Name=2;
CC IsoId=Q6NZJ6-2; Sequence=VSP_013974, VSP_013975;
CC -!- PTM: Phosphorylated at multiple sites in vivo. Phosphorylation at Ser-
CC 1187 by PRKCA induces binding to MKNK1 (By similarity). {ECO:0000250}.
CC -!- SIMILARITY: Belongs to the eukaryotic initiation factor 4G family.
CC {ECO:0000305}.
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DR EMBL; BC066038; AAH66038.1; -; mRNA.
DR EMBL; BC066103; AAH66103.1; -; mRNA.
DR EMBL; BC079675; AAH79675.1; -; mRNA.
DR EMBL; AK053144; BAC35282.1; -; mRNA.
DR CCDS; CCDS28055.1; -. [Q6NZJ6-1]
DR CCDS; CCDS84213.1; -. [Q6NZJ6-2]
DR RefSeq; NP_001291361.1; NM_001304432.1. [Q6NZJ6-2]
DR RefSeq; NP_666053.2; NM_145941.3. [Q6NZJ6-1]
DR RefSeq; XP_006522000.1; XM_006521937.1. [Q6NZJ6-1]
DR AlphaFoldDB; Q6NZJ6; -.
DR BMRB; Q6NZJ6; -.
DR SMR; Q6NZJ6; -.
DR BioGRID; 228998; 35.
DR ComplexPortal; CPX-5862; Eukaryotic translation initiation factor 4F, EIF4A2 and EIF4G1 variant.
DR ComplexPortal; CPX-5863; Eukaryotic translation initiation factor 4F, EIF4A1 and EIF4G1 variant.
DR DIP; DIP-42771N; -.
DR IntAct; Q6NZJ6; 12.
DR MINT; Q6NZJ6; -.
DR STRING; 10090.ENSMUSP00000047678; -.
DR iPTMnet; Q6NZJ6; -.
DR PhosphoSitePlus; Q6NZJ6; -.
DR SwissPalm; Q6NZJ6; -.
DR EPD; Q6NZJ6; -.
DR jPOST; Q6NZJ6; -.
DR MaxQB; Q6NZJ6; -.
DR PaxDb; Q6NZJ6; -.
DR PeptideAtlas; Q6NZJ6; -.
DR PRIDE; Q6NZJ6; -.
DR ProteomicsDB; 269377; -. [Q6NZJ6-1]
DR ProteomicsDB; 269378; -. [Q6NZJ6-2]
DR Antibodypedia; 3406; 624 antibodies from 37 providers.
DR DNASU; 208643; -.
DR Ensembl; ENSMUST00000044783; ENSMUSP00000047678; ENSMUSG00000045983. [Q6NZJ6-1]
DR Ensembl; ENSMUST00000115460; ENSMUSP00000111120; ENSMUSG00000045983. [Q6NZJ6-1]
DR Ensembl; ENSMUST00000115463; ENSMUSP00000111123; ENSMUSG00000045983. [Q6NZJ6-2]
DR GeneID; 208643; -.
DR KEGG; mmu:208643; -.
DR UCSC; uc007yqs.2; mouse. [Q6NZJ6-1]
DR UCSC; uc012acy.2; mouse. [Q6NZJ6-2]
DR CTD; 1981; -.
DR MGI; MGI:2384784; Eif4g1.
DR VEuPathDB; HostDB:ENSMUSG00000045983; -.
DR eggNOG; KOG0401; Eukaryota.
DR GeneTree; ENSGT00940000154648; -.
DR InParanoid; Q6NZJ6; -.
DR OMA; PRGGPNM; -.
DR OrthoDB; 594395at2759; -.
DR PhylomeDB; Q6NZJ6; -.
DR TreeFam; TF101527; -.
DR Reactome; R-MMU-1169408; ISG15 antiviral mechanism.
DR Reactome; R-MMU-156827; L13a-mediated translational silencing of Ceruloplasmin expression.
DR Reactome; R-MMU-166208; mTORC1-mediated signalling.
DR Reactome; R-MMU-429947; Deadenylation of mRNA.
DR Reactome; R-MMU-450408; AUF1 (hnRNP D0) binds and destabilizes mRNA.
DR Reactome; R-MMU-72649; Translation initiation complex formation.
DR Reactome; R-MMU-72662; Activation of the mRNA upon binding of the cap-binding complex and eIFs, and subsequent binding to 43S.
DR Reactome; R-MMU-72702; Ribosomal scanning and start codon recognition.
DR Reactome; R-MMU-72706; GTP hydrolysis and joining of the 60S ribosomal subunit.
DR Reactome; R-MMU-975956; Nonsense Mediated Decay (NMD) independent of the Exon Junction Complex (EJC).
DR Reactome; R-MMU-975957; Nonsense Mediated Decay (NMD) enhanced by the Exon Junction Complex (EJC).
DR BioGRID-ORCS; 208643; 7 hits in 62 CRISPR screens.
DR ChiTaRS; Eif4g1; mouse.
DR PRO; PR:Q6NZJ6; -.
DR Proteomes; UP000000589; Chromosome 16.
DR RNAct; Q6NZJ6; protein.
DR Bgee; ENSMUSG00000045983; Expressed in lacrimal gland and 254 other tissues.
DR ExpressionAtlas; Q6NZJ6; baseline and differential.
DR Genevisible; Q6NZJ6; MM.
DR GO; GO:0005737; C:cytoplasm; IDA:MGI.
DR GO; GO:0010494; C:cytoplasmic stress granule; IEA:UniProtKB-SubCell.
DR GO; GO:0005829; C:cytosol; ISO:MGI.
DR GO; GO:0016281; C:eukaryotic translation initiation factor 4F complex; ISO:MGI.
DR GO; GO:0005634; C:nucleus; ISO:MGI.
DR GO; GO:0005844; C:polysome; ISO:MGI.
DR GO; GO:0098794; C:postsynapse; ISO:MGI.
DR GO; GO:0005524; F:ATP binding; ISO:MGI.
DR GO; GO:0008190; F:eukaryotic initiation factor 4E binding; ISO:MGI.
DR GO; GO:0042802; F:identical protein binding; ISO:MGI.
DR GO; GO:0003729; F:mRNA binding; ISO:MGI.
DR GO; GO:0008135; F:translation factor activity, RNA binding; ISO:MGI.
DR GO; GO:0003743; F:translation initiation factor activity; IBA:GO_Central.
DR GO; GO:0001662; P:behavioral fear response; IGI:MGI.
DR GO; GO:0034645; P:cellular macromolecule biosynthetic process; ISO:MGI.
DR GO; GO:0031669; P:cellular response to nutrient levels; ISO:MGI.
DR GO; GO:0097009; P:energy homeostasis; ISO:MGI.
DR GO; GO:0030324; P:lung development; IEA:Ensembl.
DR GO; GO:0035278; P:miRNA-mediated gene silencing by inhibition of translation; ISO:MGI.
DR GO; GO:0010507; P:negative regulation of autophagy; ISO:MGI.
DR GO; GO:0010801; P:negative regulation of peptidyl-threonine phosphorylation; ISO:MGI.
DR GO; GO:0030182; P:neuron differentiation; IMP:MGI.
DR GO; GO:0010942; P:positive regulation of cell death; ISO:MGI.
DR GO; GO:0030307; P:positive regulation of cell growth; ISO:MGI.
DR GO; GO:1905537; P:positive regulation of eukaryotic translation initiation factor 4F complex assembly; ISO:MGI.
DR GO; GO:1900087; P:positive regulation of G1/S transition of mitotic cell cycle; ISO:MGI.
DR GO; GO:1905612; P:positive regulation of mRNA cap binding; ISO:MGI.
DR GO; GO:0045666; P:positive regulation of neuron differentiation; IMP:MGI.
DR GO; GO:0033138; P:positive regulation of peptidyl-serine phosphorylation; ISO:MGI.
DR GO; GO:0051247; P:positive regulation of protein metabolic process; ISO:MGI.
DR GO; GO:0036493; P:positive regulation of translation in response to endoplasmic reticulum stress; ISS:UniProtKB.
DR GO; GO:1905696; P:regulation of polysome binding; ISO:MGI.
DR GO; GO:1905606; P:regulation of presynapse assembly; ISO:MGI.
DR GO; GO:0006446; P:regulation of translational initiation; ISO:MGI.
DR GO; GO:0045471; P:response to ethanol; IEA:Ensembl.
DR GO; GO:0006412; P:translation; ISO:MGI.
DR GO; GO:0006413; P:translational initiation; IC:ComplexPortal.
DR InterPro; IPR016024; ARM-type_fold.
DR InterPro; IPR037584; EIF4G1.
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 PANTHER; PTHR23253:SF10; PTHR23253:SF10; 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 Acetylation; Alternative splicing; Cytoplasm; Initiation factor;
KW Methylation; Phosphoprotein; Protein biosynthesis; Reference proteome;
KW RNA-binding; Translation regulation.
FT CHAIN 1..1600
FT /note="Eukaryotic translation initiation factor 4 gamma 1"
FT /id="PRO_0000213322"
FT DOMAIN 765..993
FT /note="MIF4G"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00698"
FT DOMAIN 1241..1363
FT /note="MI"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00698"
FT DOMAIN 1429..1599
FT /note="W2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00695"
FT REGION 1..88
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 173..230
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 179..207
FT /note="PABPC1-binding"
FT /evidence="ECO:0000250"
FT REGION 243..326
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 366..501
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 507..526
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 541..606
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 611..622
FT /note="EIF4E-binding"
FT /evidence="ECO:0000250"
FT REGION 667..719
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 686..1089
FT /note="eIF3/EIF4A-binding"
FT /evidence="ECO:0000250"
FT REGION 734..760
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1029..1117
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1129..1238
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1450..1600
FT /note="EIF4A-binding"
FT /evidence="ECO:0000250"
FT REGION 1585..1600
FT /note="Necessary but not sufficient for MKNK1-binding"
FT /evidence="ECO:0000250"
FT COMPBIAS 1..26
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 30..52
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 60..74
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 181..197
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 205..228
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 267..281
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 462..481
FT /note="Acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 550..573
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 574..590
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1063..1091
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1103..1117
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1129..1143
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1144..1223
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 15
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:21183079"
FT MOD_RES 80
FT /note="Omega-N-methylarginine"
FT /evidence="ECO:0000250|UniProtKB:Q04637"
FT MOD_RES 117
FT /note="Omega-N-methylarginine"
FT /evidence="ECO:0007744|PubMed:24129315"
FT MOD_RES 214
FT /note="Phosphothreonine"
FT /evidence="ECO:0007744|PubMed:21183079"
FT MOD_RES 230
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:21183079"
FT MOD_RES 324
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q04637"
FT MOD_RES 606
FT /note="N6-acetyllysine"
FT /evidence="ECO:0007744|PubMed:23806337"
FT MOD_RES 651
FT /note="Phosphothreonine"
FT /evidence="ECO:0000250|UniProtKB:Q04637"
FT MOD_RES 689
FT /note="Omega-N-methylarginine"
FT /evidence="ECO:0007744|PubMed:24129315"
FT MOD_RES 698
FT /note="Omega-N-methylarginine"
FT /evidence="ECO:0000250|UniProtKB:Q04637"
FT MOD_RES 1032
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q04637"
FT MOD_RES 1036
FT /note="Omega-N-methylarginine"
FT /evidence="ECO:0007744|PubMed:24129315"
FT MOD_RES 1046
FT /note="Omega-N-methylarginine"
FT /evidence="ECO:0007744|PubMed:24129315"
FT MOD_RES 1081
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q04637"
FT MOD_RES 1096
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:21183079"
FT MOD_RES 1099
FT /note="N6-acetyllysine"
FT /evidence="ECO:0000250|UniProtKB:Q04637"
FT MOD_RES 1147
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q04637"
FT MOD_RES 1149
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q04637"
FT MOD_RES 1187
FT /note="Phosphoserine; by PKC/PRKCA"
FT /evidence="ECO:0000250|UniProtKB:Q04637"
FT MOD_RES 1189
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:19144319"
FT MOD_RES 1196
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q04637"
FT MOD_RES 1211
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:18630941,
FT ECO:0007744|PubMed:21183079"
FT MOD_RES 1213
FT /note="Phosphothreonine"
FT /evidence="ECO:0000250|UniProtKB:Q04637"
FT MOD_RES 1231
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:17242355,
FT ECO:0007744|PubMed:19131326, ECO:0007744|PubMed:19144319"
FT MOD_RES 1238
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q04637"
FT MOD_RES 1597
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:19131326"
FT VAR_SEQ 49..55
FT /note="Missing (in isoform 2)"
FT /evidence="ECO:0000303|PubMed:15489334,
FT ECO:0000303|PubMed:16141072"
FT /id="VSP_013974"
FT VAR_SEQ 1046..1052
FT /note="Missing (in isoform 2)"
FT /evidence="ECO:0000303|PubMed:15489334,
FT ECO:0000303|PubMed:16141072"
FT /id="VSP_013975"
SQ SEQUENCE 1600 AA; 176077 MW; 8664A8B449C7A128 CRC64;
MNKAPQPTGP PPARSPGLPQ PAFPPGQTAP VVFSTPQATQ MNTPSQPRQG GFRSLQHFYP
SRAQPPSSAA SRVQSAAPAR PGPAPHVYPA GSQVMMIPSQ ISYSASQGAY YIPGQGRSTY
VVPTQQYPVQ PGAPGFYPGA SPTEFGTYAG AYYPAQGVQQ FPASVAPAPV LMNQPPQIAP
KRERKTIRIR DPNQGGKDIT EEIMSGARTA STPTPPQTGG SLEPQPNGES PQVAVIIRPD
DRSQGAAIGG RPGLPGPEHS PGTESQPSSP SPTPSPPPIL EPGSESNLGV LSIPGDTMTT
GMIPMSVEES TPISCETGEP YCLSPEPTLA EPILEVEVTL SKPIPESEFS SSPLQVSTAL
VPHKVETHEP NGVIPSEDLE PEVESSTEPA PPPLSPCASE SLVPIAPTAQ PEELLNGAPS
PPAVDLSPVS EPEEQAKKVS SAALASILSP APPVAPSDTS PAQEEEMEED DDDEEGGEAE
SEKGGEDVPL DSTPVPAQLS QNLEVAAATQ VAVSVPKRRR KIKELNKKEA VGDLLDAFKE
VDPAVPEVEN QPPTGSNPSP ESEGSMVPTQ PEETEETWDS KEDKIHNAEN IQPGEQKYEY
KSDQWKPLNL EEKKRYDREF LLGFQFIFAS MQKPEGLPHI TDVVLDKANK TPLRQLDPSR
LPGINCGPDF TPSFANLGRP ALSNRGPPRG GPGGELPRGP AGLGPRRSQQ GPRKETRKII
SSVIMTEDIK LNKAEKAWKP SSKRTAADKD RGEEDADGSK TQDLFRRVRS ILNKLTPQMF
QQLMKQVTQL AIDTEERLKG VIDLIFEKAI SEPNFSVAYA NMCRCLMALK VPTTEKPTVT
VNFRKLLLNR CQKEFEKDKD DDEVFEKKQK EMDEAATAEE RGRLKEELEE ARDIARRRSL
GNIKFIGELF KLKMLTEAIM HDCVVKLLKN HDEESLECLC RLLTTIGKDL DFAKAKPRMD
QYFNQMEKII KEKKTSSRIR FMLQDVLDLR QSNWVPRRGD QGPKTIDQIH KEAEMEEHRE
HIKVQQLMAK GSDKRRGGPP GPPINRGLPL VDDGGWNTVP ISKGSRPIDT SRLTKITKPG
SIDSNNQLFA PGGRLSWGKG SSGGSGAKPS DTASEATRPA TLNRFSALQQ TLPAENTDNR
RVVQRSSLSR ERGEKAGDRG DRLERSERGG DRGDRLDRAR TPATKRSFSK EVEERSRERP
SQPEGLRKAA SLTEDRGRDP VKREATLPPV SPPKAALSVD EVEKKSKAII EEYLHLNDMK
EAVQCVQELA SPSLLFIFVR LGIESTLERS TIAREHMGRL LHQLLCAGHL STAQYYQGLY
ETLELAEDME IDIPHVWLYL AELITPILQE DGVPMGELFR EITKPLRPMG KATSLLLEIL
GLLCKSMGPK KVGMLWREAG LSWREFLAEG QDVGSFVAEK KVEYTLGEES EAPGQRTLAF
EELRRQLEKL LKDGGSNQRV FDWIDANLNE QQIASNTLVR ALMTTVCYSA IIFETPLRVD
VQVLKVRARL LQKYLCDEQK ELQALYALQA LVVTLEQPAN LLRMFFDALY DEDVVKEDAF
YSWESSKDPA EQQGKGVALK SVTAFFNWLR EAEDEESDHN
