IF4E_MOUSE
ID IF4E_MOUSE Reviewed; 217 AA.
AC P63073; P20415;
DT 13-SEP-2004, integrated into UniProtKB/Swiss-Prot.
DT 13-SEP-2004, sequence version 1.
DT 03-AUG-2022, entry version 161.
DE RecName: Full=Eukaryotic translation initiation factor 4E {ECO:0000303|PubMed:2663851};
DE Short=eIF-4E {ECO:0000303|PubMed:2663851};
DE Short=eIF4E {ECO:0000303|PubMed:2663851};
DE Short=mRNA cap-binding protein;
DE AltName: Full=eIF-4F 25 kDa subunit;
GN Name=Eif4e {ECO:0000303|PubMed:2663851, ECO:0000312|MGI:MGI:95305};
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 [MRNA].
RX PubMed=2663851; DOI=10.1016/s0021-9258(18)63833-5;
RA Altmann M., Mueller P.P., Pelletier J., Sonenberg N., Trachsel H.;
RT "A mammalian translation initiation factor can substitute for its yeast
RT homologue in vivo.";
RL J. Biol. Chem. 264:12145-12147(1989).
RN [2]
RP NUCLEOTIDE SEQUENCE [MRNA].
RX PubMed=2037592; DOI=10.1016/s0021-9258(18)99245-8;
RA Jaramillo M., Pelletier J., Edery I., Nielsen P.J., Sonenberg N.;
RT "Multiple mRNAs encode the murine translation initiation factor eIF-4E.";
RL J. Biol. Chem. 266:10446-10451(1991).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=FVB/N; TISSUE=Colon, and Mammary gland;
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 [4]
RP INTERACTION WITH NGDN.
RX PubMed=16705177; DOI=10.1128/mcb.02470-05;
RA Jung M.-Y., Lorenz L., Richter J.D.;
RT "Translational control by neuroguidin, a eukaryotic initiation factor 4E
RT and CPEB binding protein.";
RL Mol. Cell. Biol. 26:4277-4287(2006).
RN [5]
RP PHOSPHORYLATION AT SER-209 BY MKNK2.
RX PubMed=17689282; DOI=10.1016/j.biocel.2007.05.001;
RA Shenberger J.S., Zhang L., Hughlock M.K., Ueda T., Watanabe-Fukunaga R.,
RA Fukunaga R.;
RT "Roles of mitogen-activated protein kinase signal-integrating kinases 1 and
RT 2 in oxidant-mediated eIF4E phosphorylation.";
RL Int. J. Biochem. Cell Biol. 39:1828-1842(2007).
RN [6]
RP FUNCTION, INTERACTION WITH CYFIP1 AND FMR1, AND MUTAGENESIS OF TRP-73.
RX PubMed=18805096; DOI=10.1016/j.cell.2008.07.031;
RA Napoli I., Mercaldo V., Boyl P.P., Eleuteri B., Zalfa F., De Rubeis S.,
RA Di Marino D., Mohr E., Massimi M., Falconi M., Witke W., Costa-Mattioli M.,
RA Sonenberg N., Achsel T., Bagni C.;
RT "The fragile X syndrome protein represses activity-dependent translation
RT through CYFIP1, a new 4E-BP.";
RL Cell 134:1042-1054(2008).
RN [7]
RP INTERACTION WITH PIWIL2.
RX PubMed=19114715; DOI=10.1074/jbc.m809104200;
RA Unhavaithaya Y., Hao Y., Beyret E., Yin H., Kuramochi-Miyagawa S.,
RA Nakano T., Lin H.;
RT "MILI, a PIWI-interacting RNA-binding protein, is required for germ Line
RT stem cell self-renewal and appears to positively regulate translation.";
RL J. Biol. Chem. 284:6507-6519(2009).
RN [8]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Brain, Heart, Kidney, Liver, Lung, Pancreas, 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 SUBCELLULAR LOCATION, AND INTERACTION WITH CLOCK.
RX PubMed=22900038; DOI=10.1371/journal.pone.0042695;
RA Peruquetti R.L., de Mateo S., Sassone-Corsi P.;
RT "Circadian proteins CLOCK and BMAL1 in the chromatoid body, a RNA
RT processing granule of male germ cells.";
RL PLoS ONE 7:E42695-E42695(2012).
RN [10]
RP FUNCTION.
RX PubMed=25456498; DOI=10.1016/j.neuron.2014.10.022;
RA Yang G., Smibert C.A., Kaplan D.R., Miller F.D.;
RT "An eIF4E1/4E-T complex determines the genesis of neurons from precursors
RT by translationally repressing a proneurogenic transcription program.";
RL Neuron 84:723-739(2014).
RN [11]
RP INTERACTION WITH BTG4 AND CNOT7.
RX PubMed=27065194; DOI=10.1038/nsmb.3204;
RA Yu C., Ji S.Y., Sha Q.Q., Dang Y., Zhou J.J., Zhang Y.L., Liu Y.,
RA Wang Z.W., Hu B., Sun Q.Y., Sun S.C., Tang F., Fan H.Y.;
RT "BTG4 is a meiotic cell cycle-coupled maternal-zygotic-transition licensing
RT factor in oocytes.";
RL Nat. Struct. Mol. Biol. 23:387-394(2016).
RN [12]
RP X-RAY CRYSTALLOGRAPHY (2.20 ANGSTROMS) OF 28-217 IN COMPLEX WITH MRNA CAP
RP ANALOG.
RX PubMed=9200613; DOI=10.1016/s0092-8674(00)80280-9;
RA Marcotrigiano J., Gingras A.-C., Sonenberg N., Burley S.K.;
RT "Cocrystal structure of the messenger RNA 5' cap-binding protein (eIF4E)
RT bound to 7-methyl-GDP.";
RL Cell 89:951-961(1997).
RN [13]
RP X-RAY CRYSTALLOGRAPHY (2.25 ANGSTROMS) OF 28-217 IN COMPLEX WITH MRNA CAP
RP ANALOG AND EIF4EBP1.
RX PubMed=10394359; DOI=10.1016/s1097-2765(01)80003-4;
RA Marcotrigiano J., Gingras A.-C., Sonenberg N., Burley S.K.;
RT "Cap-dependent translation initiation in eukaryotes is regulated by a
RT molecular mimic of eIF4G.";
RL Mol. Cell 3:707-716(1999).
CC -!- FUNCTION: Recognizes and binds the 7-methylguanosine-containing mRNA
CC cap during an early step in the initiation of protein synthesis and
CC facilitates ribosome binding by inducing the unwinding of the mRNAs
CC secondary structures (By similarity). In addition to its role in
CC translation initiation, also acts as a regulator of translation and
CC stability in the cytoplasm (PubMed:18805096, PubMed:25456498).
CC Component of the CYFIP1-EIF4E-FMR1 complex which binds to the mRNA cap
CC and mediates translational repression: in the complex, EIF4E mediates
CC the binding to the mRNA cap (PubMed:18805096). Component of a
CC multiprotein complex that sequesters and represses translation of
CC proneurogenic factors during neurogenesis (PubMed:25456498). In P-
CC bodies, component of a complex that mediates the storage of
CC translationally inactive mRNAs in the cytoplasm and prevents their
CC degradation (By similarity). May play an important role in
CC spermatogenesis through translational regulation of stage-specific
CC mRNAs during germ cell development (By similarity).
CC {ECO:0000250|UniProtKB:P06730, ECO:0000250|UniProtKB:P63074,
CC ECO:0000269|PubMed:18805096, ECO:0000269|PubMed:25456498}.
CC -!- SUBUNIT: eIF4F is a multi-subunit complex, the composition of which
CC varies with external and internal environmental conditions (By
CC similarity). It is composed of at least EIF4A, EIF4E and EIF4G1/EIF4G3
CC (PubMed:9200613). EIF4E is also known to interact with other partners
CC (By similarity). Interacts with EIF4ENIF1/4E-T; promotes recruitment to
CC P-bodies and import into the nucleus (By similarity).
CC Hypophosphorylated EIF4EBP1, EIF4EBP2 and EIF4EBP3 compete with
CC EIF4G1/EIF4G3 to interact with EIF4E; insulin stimulated MAP-kinase
CC (MAPK1 and MAPK3) phosphorylation of EIF4EBP1 causes dissociation of
CC the complex allowing EIF4G1/EIF4G3 to bind and consequent initiation of
CC translation (PubMed:10394359). Interacts mutually exclusive with EIF4A1
CC or EIF4A2 (By similarity). Interacts with NGDN and PIWIL2
CC (PubMed:16705177, PubMed:19114715). Component of the CYFIP1-EIF4E-FMR1
CC complex composed of CYFIP, EIF4E and FMR1 (PubMed:18805096). Interacts
CC directly with CYFIP1 (PubMed:18805096). Interacts with CLOCK
CC (PubMed:22900038). Binds to MKNK2 in nucleus (By similarity). Interacts
CC with LIMD1, WTIP and AJUBA (By similarity). Interacts with APOBEC3G in
CC an RNA-dependent manner (By similarity). Interacts with LARP1 (By
CC similarity). Interacts with METTL3 (By similarity). Interacts with
CC RBM24; this interaction prevents EIF4E from binding to p53/TP53 mRNA
CC and inhibits the assembly of translation initiation complex (By
CC similarity). Interacts with DDX3X; interaction is direct and in an RNA-
CC independent manner; this interaction enhances EIF4E cap-binding ability
CC and is required for the repression of cap-dependent translation and the
CC increase of IRES-mediated translation (By similarity). DDX3X competes
CC with EIF4G1 for interaction with EIF4E (By similarity). Interacts with
CC BTG4 and CNOT7 (PubMed:27065194). {ECO:0000250|UniProtKB:P06730,
CC ECO:0000269|PubMed:10394359, ECO:0000269|PubMed:16705177,
CC ECO:0000269|PubMed:18805096, ECO:0000269|PubMed:19114715,
CC ECO:0000269|PubMed:22900038, ECO:0000269|PubMed:27065194,
CC ECO:0000269|PubMed:9200613}.
CC -!- INTERACTION:
CC P63073; Q7TMB8: Cyfip1; NbExp=5; IntAct=EBI-2000006, EBI-772928;
CC P63073; Q60876: Eif4ebp1; NbExp=3; IntAct=EBI-2000006, EBI-398674;
CC P63073; Q6NZJ6: Eif4g1; NbExp=7; IntAct=EBI-2000006, EBI-8175606;
CC P63073; Q7L576: CYFIP1; Xeno; NbExp=2; IntAct=EBI-2000006, EBI-1048143;
CC -!- SUBCELLULAR LOCATION: Cytoplasm, P-body {ECO:0000250|UniProtKB:P06730}.
CC Cytoplasm {ECO:0000269|PubMed:22900038}. Cytoplasm, Stress granule
CC {ECO:0000250|UniProtKB:P06730}. Nucleus {ECO:0000250|UniProtKB:P06730}.
CC Note=Interaction with EIF4ENIF1/4E-T is required for localization to
CC processing bodies (P-bodies). Imported in the nucleus via interaction
CC with EIF4ENIF1/4E-T via a piggy-back mechanism.
CC {ECO:0000250|UniProtKB:P06730}.
CC -!- PTM: Phosphorylation increases the ability of the protein to bind to
CC mRNA caps and to form the eIF4F complex.
CC {ECO:0000250|UniProtKB:P06730}.
CC -!- SIMILARITY: Belongs to the eukaryotic initiation factor 4E family.
CC {ECO:0000305}.
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DR EMBL; M61731; AAA37545.1; -; mRNA.
DR EMBL; BC010759; AAH10759.1; -; mRNA.
DR EMBL; BC085087; AAH85087.1; -; mRNA.
DR CCDS; CCDS38654.1; -.
DR PIR; A34295; A34295.
DR PIR; I49644; I49644.
DR RefSeq; NP_031943.3; NM_007917.4.
DR PDB; 1EJ1; X-ray; 2.20 A; A/B=28-217.
DR PDB; 1EJ4; X-ray; 2.25 A; A=28-217.
DR PDB; 1EJH; X-ray; 2.20 A; A/B/C/D=28-217.
DR PDB; 1L8B; X-ray; 1.80 A; A/B=28-217.
DR PDB; 5BXV; X-ray; 2.10 A; A/C=27-217.
DR PDB; 5J5O; X-ray; 1.87 A; A/B/C/D=28-217.
DR PDB; 5J5Y; X-ray; 1.75 A; A/B/C/D=28-217.
DR PDB; 5M7V; X-ray; 1.74 A; A/B/C/D=28-217.
DR PDB; 5M7W; X-ray; 1.97 A; A/B/C/D=28-217.
DR PDB; 5M7X; X-ray; 1.68 A; A/B/C/D=28-217.
DR PDB; 5M7Z; X-ray; 1.69 A; A/B/C/D=28-217.
DR PDB; 5M80; X-ray; 2.12 A; A/B/C/D=28-217.
DR PDB; 5M81; X-ray; 1.90 A; A/B/C/D=28-217.
DR PDB; 5M83; X-ray; 1.86 A; A/B=28-217.
DR PDB; 5M84; X-ray; 1.85 A; A/B=28-217.
DR PDB; 5OSX; X-ray; 1.92 A; A/B/C/D=28-217.
DR PDB; 6GKJ; X-ray; 2.07 A; A/B/C/D=28-217.
DR PDB; 6GKK; X-ray; 1.86 A; A/B/C/D=28-217.
DR PDB; 6GKL; X-ray; 2.20 A; A/B/C/D=28-217.
DR PDB; 6U06; X-ray; 1.96 A; A/B/C/D=28-217.
DR PDB; 6U09; X-ray; 1.79 A; A/B/C/D=28-217.
DR PDB; 6YLR; X-ray; 2.20 A; A/B=28-217.
DR PDB; 6YLT; X-ray; 2.67 A; A/B/C/D=28-217.
DR PDB; 6YLV; X-ray; 2.66 A; A/B/C/D=28-217.
DR PDBsum; 1EJ1; -.
DR PDBsum; 1EJ4; -.
DR PDBsum; 1EJH; -.
DR PDBsum; 1L8B; -.
DR PDBsum; 5BXV; -.
DR PDBsum; 5J5O; -.
DR PDBsum; 5J5Y; -.
DR PDBsum; 5M7V; -.
DR PDBsum; 5M7W; -.
DR PDBsum; 5M7X; -.
DR PDBsum; 5M7Z; -.
DR PDBsum; 5M80; -.
DR PDBsum; 5M81; -.
DR PDBsum; 5M83; -.
DR PDBsum; 5M84; -.
DR PDBsum; 5OSX; -.
DR PDBsum; 6GKJ; -.
DR PDBsum; 6GKK; -.
DR PDBsum; 6GKL; -.
DR PDBsum; 6U06; -.
DR PDBsum; 6U09; -.
DR PDBsum; 6YLR; -.
DR PDBsum; 6YLT; -.
DR PDBsum; 6YLV; -.
DR AlphaFoldDB; P63073; -.
DR BMRB; P63073; -.
DR SMR; P63073; -.
DR BioGRID; 199420; 64.
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 ComplexPortal; CPX-5864; Eukaryotic translation initiation factor 4F, EIF4A2 and EIF4G3 variant.
DR ComplexPortal; CPX-5865; Eukaryotic translation initiation factor 4F, EIF4A1 and EIF4G3 variant.
DR DIP; DIP-42768N; -.
DR IntAct; P63073; 13.
DR MINT; P63073; -.
DR STRING; 10090.ENSMUSP00000029803; -.
DR BindingDB; P63073; -.
DR ChEMBL; CHEMBL6148; -.
DR iPTMnet; P63073; -.
DR PhosphoSitePlus; P63073; -.
DR REPRODUCTION-2DPAGE; P63073; -.
DR EPD; P63073; -.
DR jPOST; P63073; -.
DR PaxDb; P63073; -.
DR PeptideAtlas; P63073; -.
DR PRIDE; P63073; -.
DR ProteomicsDB; 267212; -.
DR Antibodypedia; 3421; 1000 antibodies from 45 providers.
DR DNASU; 13684; -.
DR Ensembl; ENSMUST00000029803; ENSMUSP00000029803; ENSMUSG00000028156.
DR GeneID; 13684; -.
DR KEGG; mmu:13684; -.
DR UCSC; uc008rnn.1; mouse.
DR CTD; 1977; -.
DR MGI; MGI:95305; Eif4e.
DR VEuPathDB; HostDB:ENSMUSG00000028156; -.
DR eggNOG; KOG1670; Eukaryota.
DR GeneTree; ENSGT00940000154194; -.
DR HOGENOM; CLU_043552_1_1_1; -.
DR InParanoid; P63073; -.
DR OMA; EEFWAIV; -.
DR PhylomeDB; P63073; -.
DR TreeFam; TF101526; -.
DR Reactome; R-MMU-1169408; ISG15 antiviral mechanism.
DR Reactome; R-MMU-156827; L13a-mediated translational silencing of Ceruloplasmin expression.
DR Reactome; R-MMU-159227; Transport of the SLBP independent Mature mRNA.
DR Reactome; R-MMU-159230; Transport of the SLBP Dependant Mature mRNA.
DR Reactome; R-MMU-159231; Transport of Mature mRNA Derived from an Intronless Transcript.
DR Reactome; R-MMU-166208; mTORC1-mediated signalling.
DR Reactome; R-MMU-429947; Deadenylation of 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 BioGRID-ORCS; 13684; 25 hits in 70 CRISPR screens.
DR ChiTaRS; Eif4e; mouse.
DR EvolutionaryTrace; P63073; -.
DR PRO; PR:P63073; -.
DR Proteomes; UP000000589; Chromosome 3.
DR RNAct; P63073; protein.
DR Bgee; ENSMUSG00000028156; Expressed in retinal neural layer and 258 other tissues.
DR ExpressionAtlas; P63073; baseline and differential.
DR Genevisible; P63073; MM.
DR GO; GO:0033391; C:chromatoid body; IDA:MGI.
DR GO; GO:0005737; C:cytoplasm; IDA:MGI.
DR GO; GO:0036464; C:cytoplasmic ribonucleoprotein granule; ISO:MGI.
DR GO; GO:0010494; C:cytoplasmic stress granule; ISS:UniProtKB.
DR GO; GO:0005829; C:cytosol; ISS:UniProtKB.
DR GO; GO:0016281; C:eukaryotic translation initiation factor 4F complex; ISS:UniProtKB.
DR GO; GO:0098978; C:glutamatergic synapse; IDA:SynGO.
DR GO; GO:0005845; C:mRNA cap binding complex; IDA:UniProtKB.
DR GO; GO:0005634; C:nucleus; IEA:UniProtKB-SubCell.
DR GO; GO:0000932; C:P-body; ISS:UniProtKB.
DR GO; GO:0048471; C:perinuclear region of cytoplasm; ISS:AgBase.
DR GO; GO:0098794; C:postsynapse; ISO:MGI.
DR GO; GO:0099524; C:postsynaptic cytosol; ISO:MGI.
DR GO; GO:0032991; C:protein-containing complex; ISO:MGI.
DR GO; GO:0016442; C:RISC complex; ISO:MGI.
DR GO; GO:0140297; F:DNA-binding transcription factor binding; ISS:AgBase.
DR GO; GO:0019899; F:enzyme binding; ISS:AgBase.
DR GO; GO:0031370; F:eukaryotic initiation factor 4G binding; ISS:AgBase.
DR GO; GO:0000340; F:RNA 7-methylguanosine cap binding; ISS:UniProtKB.
DR GO; GO:0003743; F:translation initiation factor activity; IDA:UniProtKB.
DR GO; GO:0045182; F:translation regulator activity; IDA:SynGO.
DR GO; GO:0001662; P:behavioral fear response; IGI:MGI.
DR GO; GO:0071549; P:cellular response to dexamethasone stimulus; IDA:MGI.
DR GO; GO:0000082; P:G1/S transition of mitotic cell cycle; ISO:MGI.
DR GO; GO:0045665; P:negative regulation of neuron differentiation; IMP:MGI.
DR GO; GO:0017148; P:negative regulation of translation; IMP:MGI.
DR GO; GO:0030182; P:neuron differentiation; IMP:MGI.
DR GO; GO:0045931; P:positive regulation of mitotic cell cycle; ISO:MGI.
DR GO; GO:0006417; P:regulation of translation; ISS:UniProtKB.
DR GO; GO:0099578; P:regulation of translation at postsynapse, modulating synaptic transmission; IDA:SynGO.
DR GO; GO:0019827; P:stem cell population maintenance; IMP:MGI.
DR GO; GO:0006412; P:translation; IMP:MGI.
DR GO; GO:0006413; P:translational initiation; IC:ComplexPortal.
DR Gene3D; 3.30.760.10; -; 1.
DR IDEAL; IID50218; -.
DR InterPro; IPR023398; TIF_eIF4e-like.
DR InterPro; IPR001040; TIF_eIF_4E.
DR InterPro; IPR019770; TIF_eIF_4E_CS.
DR PANTHER; PTHR11960; PTHR11960; 1.
DR Pfam; PF01652; IF4E; 1.
DR SUPFAM; SSF55418; SSF55418; 1.
DR PROSITE; PS00813; IF4E; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Acetylation; Cytoplasm; Initiation factor; Nucleus;
KW Phosphoprotein; Protein biosynthesis; Reference proteome; RNA-binding;
KW Translation regulation.
FT INIT_MET 1
FT /note="Removed"
FT /evidence="ECO:0000250|UniProtKB:P06730"
FT CHAIN 2..217
FT /note="Eukaryotic translation initiation factor 4E"
FT /id="PRO_0000193635"
FT REGION 1..27
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 37..40
FT /note="EIF4EBP1/2/3 binding"
FT /evidence="ECO:0000269|PubMed:10394359"
FT REGION 73..77
FT /note="EIF4EBP1/2/3 binding"
FT /evidence="ECO:0000269|PubMed:10394359"
FT REGION 132..139
FT /note="EIF4EBP1/2/3 binding"
FT /evidence="ECO:0000269|PubMed:10394359"
FT COMPBIAS 1..19
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 56..57
FT /ligand="mRNA"
FT /ligand_id="ChEBI:CHEBI:33699"
FT /ligand_part="N(7)-methylguanosine 5'-triphosphate group"
FT /ligand_part_id="ChEBI:CHEBI:74429"
FT /ligand_part_note="m7GTP residue in mRNA cap"
FT /evidence="ECO:0000269|PubMed:10394359,
FT ECO:0000269|PubMed:9200613"
FT BINDING 102..103
FT /ligand="mRNA"
FT /ligand_id="ChEBI:CHEBI:33699"
FT /ligand_part="N(7)-methylguanosine 5'-triphosphate group"
FT /ligand_part_id="ChEBI:CHEBI:74429"
FT /ligand_part_note="m7GTP residue in mRNA cap"
FT /evidence="ECO:0000269|PubMed:10394359,
FT ECO:0000269|PubMed:9200613"
FT BINDING 157..162
FT /ligand="mRNA"
FT /ligand_id="ChEBI:CHEBI:33699"
FT /ligand_part="N(7)-methylguanosine 5'-triphosphate group"
FT /ligand_part_id="ChEBI:CHEBI:74429"
FT /ligand_part_note="m7GTP residue in mRNA cap"
FT /evidence="ECO:0000269|PubMed:10394359,
FT ECO:0000269|PubMed:9200613"
FT BINDING 205..207
FT /ligand="mRNA"
FT /ligand_id="ChEBI:CHEBI:33699"
FT /ligand_part="N(7)-methylguanosine 5'-triphosphate group"
FT /ligand_part_id="ChEBI:CHEBI:74429"
FT /ligand_part_note="m7GTP residue in mRNA cap"
FT /evidence="ECO:0000269|PubMed:10394359,
FT ECO:0000269|PubMed:9200613"
FT MOD_RES 2
FT /note="N-acetylalanine"
FT /evidence="ECO:0000250|UniProtKB:P06730"
FT MOD_RES 22
FT /note="Phosphothreonine"
FT /evidence="ECO:0000250|UniProtKB:P06730"
FT MOD_RES 209
FT /note="Phosphoserine; by PKC and MKNK2"
FT /evidence="ECO:0000269|PubMed:17689282"
FT MUTAGEN 73
FT /note="W->A: Binding to CYFIP1 reduced by 70%."
FT /evidence="ECO:0000269|PubMed:18805096"
FT CONFLICT 70
FT /note="E -> L (in Ref. 1; no nucleotide entry)"
FT /evidence="ECO:0000305"
FT HELIX 31..33
FT /evidence="ECO:0007829|PDB:5M7X"
FT STRAND 38..48
FT /evidence="ECO:0007829|PDB:5M7X"
FT STRAND 52..54
FT /evidence="ECO:0007829|PDB:1L8B"
FT HELIX 57..59
FT /evidence="ECO:0007829|PDB:5M7X"
FT STRAND 60..68
FT /evidence="ECO:0007829|PDB:5M7X"
FT HELIX 69..78
FT /evidence="ECO:0007829|PDB:5M7X"
FT HELIX 82..84
FT /evidence="ECO:0007829|PDB:5M7X"
FT STRAND 90..95
FT /evidence="ECO:0007829|PDB:5M7X"
FT TURN 105..109
FT /evidence="ECO:0007829|PDB:5M7X"
FT STRAND 111..116
FT /evidence="ECO:0007829|PDB:5M7X"
FT HELIX 121..124
FT /evidence="ECO:0007829|PDB:5M7X"
FT HELIX 126..138
FT /evidence="ECO:0007829|PDB:5M7X"
FT TURN 139..142
FT /evidence="ECO:0007829|PDB:5M7X"
FT HELIX 143..148
FT /evidence="ECO:0007829|PDB:5M7X"
FT STRAND 149..155
FT /evidence="ECO:0007829|PDB:5M7X"
FT STRAND 162..168
FT /evidence="ECO:0007829|PDB:5M7X"
FT HELIX 173..187
FT /evidence="ECO:0007829|PDB:5M7X"
FT TURN 191..193
FT /evidence="ECO:0007829|PDB:1EJH"
FT STRAND 195..199
FT /evidence="ECO:0007829|PDB:5M7X"
FT HELIX 200..203
FT /evidence="ECO:0007829|PDB:5M7X"
FT STRAND 208..210
FT /evidence="ECO:0007829|PDB:1EJ1"
FT STRAND 214..217
FT /evidence="ECO:0007829|PDB:5M7X"
SQ SEQUENCE 217 AA; 25053 MW; FC61D0FB337BCD8F CRC64;
MATVEPETTP TTNPPPAEEE KTESNQEVAN PEHYIKHPLQ NRWALWFFKN DKSKTWQANL
RLISKFDTVE DFWALYNHIQ LSSNLMPGCD YSLFKDGIEP MWEDEKNKRG GRWLITLNKQ
QRRSDLDRFW LETLLCLIGE SFDDYSDDVC GAVVNVRAKG DKIAIWTTEC ENRDAVTHIG
RVYKERLGLP PKIVIGYQSH ADTATKSGST TKNRFVV
