{"results":[{"entryType":"UniProtKB reviewed (Swiss-Prot)","primaryAccession":"P06730","secondaryAccessions":["B7Z6V1","D6RCQ6","Q96E95"],"uniProtkbId":"IF4E_HUMAN","entryAudit":{"firstPublicDate":"1988-01-01","lastAnnotationUpdateDate":"2026-09-02","lastSequenceUpdateDate":"1996-02-01","entryVersion":251,"sequenceVersion":2},"annotationScore":5.0,"organism":{"scientificName":"Homo sapiens","commonName":"Human","taxonId":9606,"lineage":["Eukaryota","Metazoa","Chordata","Craniata","Vertebrata","Euteleostomi","Mammalia","Eutheria","Euarchontoglires","Primates","Haplorrhini","Catarrhini","Hominidae","Homo"]},"proteinExistence":"1: Evidence at protein level","proteinDescription":{"recommendedName":{"fullName":{"evidences":[{"evidenceCode":"ECO:0000303","source":"PubMed","id":"1993647"}],"value":"Eukaryotic translation initiation factor 4E"},"shortNames":[{"value":"eIF-4E"},{"evidences":[{"evidenceCode":"ECO:0000303","source":"PubMed","id":"29987188"}],"value":"eIF4E"}]},"alternativeNames":[{"fullName":{"value":"eIF-4F 25 kDa subunit"}},{"fullName":{"evidences":[{"evidenceCode":"ECO:0000303","source":"PubMed","id":"3469651"}],"value":"mRNA cap-binding protein"}}]},"genes":[{"geneName":{"evidences":[{"evidenceCode":"ECO:0000312","source":"HGNC","id":"HGNC:3287"}],"value":"EIF4E"},"synonyms":[{"value":"EIF4EL1"},{"value":"EIF4F"}]}],"comments":[{"texts":[{"evidences":[{"evidenceCode":"ECO:0000250","source":"UniProtKB","id":"P63073"},{"evidenceCode":"ECO:0000250","source":"UniProtKB","id":"P63074"},{"evidenceCode":"ECO:0000269","source":"PubMed","id":"11606200"},{"evidenceCode":"ECO:0000269","source":"PubMed","id":"16271312"},{"evidenceCode":"ECO:0000269","source":"PubMed","id":"22578813"},{"evidenceCode":"ECO:0000269","source":"PubMed","id":"22684010"},{"evidenceCode":"ECO:0000269","source":"PubMed","id":"23471078"},{"evidenceCode":"ECO:0000269","source":"PubMed","id":"24335285"},{"evidenceCode":"ECO:0000269","source":"PubMed","id":"29987188"}],"value":"Acts in the cytoplasm to initiate and regulate protein synthesis and is required in the nucleus for export of a subset of mRNAs from the nucleus to the cytoplasm which promotes processes such as RNA capping, processing and splicing (PubMed:11606200, PubMed:22578813, PubMed:22684010, PubMed:24335285, PubMed:29987188). Component of the protein complex eIF4F, which is involved in the recognition of the mRNA cap, ATP-dependent unwinding of 5'-terminal secondary structure and recruitment of mRNA to the ribosome (By similarity). This protein recognizes and binds the 7-methylguanosine (m7G)-containing mRNA cap during an early step in the initiation of protein synthesis and facilitates ribosome binding by inducing the unwinding of the mRNAs secondary structures (PubMed:16271312, PubMed:22578813). Together with EIF4G1, antagonizes the scanning promoted by EIF1-EIF4G1 and is required for TISU translation, a process where the TISU element recognition makes scanning unnecessary (PubMed:29987188). In addition to its role in translation initiation, also acts as a regulator of translation and stability in the cytoplasm (PubMed:24335285). Component of the CYFIP1-EIF4E-FMR1 complex which binds to the mRNA cap and mediates translational repression: in the complex, EIF4E mediates the binding to the mRNA cap (By similarity). Component of a multiprotein complex that sequesters and represses translation of proneurogenic factors during neurogenesis (By similarity). In P-bodies, component of a complex that mediates the storage of translationally inactive mRNAs in the cytoplasm and prevents their degradation (PubMed:24335285). May play an important role in spermatogenesis through translational regulation of stage-specific mRNAs during germ cell development (By similarity). As well as its roles in translation, also involved in mRNA nucleocytoplasmic transport (By similarity). Its role in mRNA export from the nucleus to the cytoplasm relies on its ability to bind the m7G cap of RNAs and on the presence of the 50-nucleotide EIF4E sensitivity element (4ESE) in the 3'UTR of sensitive transcripts (By similarity). Interaction with the 4ESE is mediated by LRPPRC which binds simultaneously to both EIF4E and the 4ESE, thereby acting as a platform for assembly for the RNA export complex (By similarity). EIF4E-dependent mRNA export is independent of ongoing protein or RNA synthesis and is also NFX1-independent but is XPO1-dependent with LRPPRC interacting with XPO1 to form an EIF4E-dependent mRNA export complex (By similarity). Alters the composition of the cytoplasmic face of the nuclear pore to promote RNA export by reducing RANBP2 expression, relocalizing nucleoporin NUP214 and increasing expression of RANBP1 and RNA export factors DDX19 and GLE1 (By similarity). Promotes the nuclear export of cyclin CCND1 mRNA (By similarity). Promotes the nuclear export of NOS2/iNOS mRNA (PubMed:23471078). Promotes the nuclear export of MDM2 mRNA (PubMed:22684010). Promotes the export of additional mRNAs, including others involved in the cell cycle (By similarity). In the nucleus, binds to capped splice factor-encoding mRNAs and stimulates their nuclear export to enhance splice factor production by increasing their cytoplasmic availability to the translation machinery (By similarity). May also regulate splicing through interaction with the spliceosome in an RNA and m7G cap-dependent manner (By similarity). Also binds to some pre-mRNAs and may play a role in their recruitment to the spliceosome (By similarity). Promotes steady-state capping of a subset of coding and non-coding RNAs by mediating nuclear export of capping machinery mRNAs including RNMT, RNGTT and RAMAC to enhance their translation (By similarity). Stimulates mRNA 3'-end processing by promoting the expression of several core cleavage complex factors required for mRNA cleavage and polyadenylation, and may also have a direct effect through its interaction with the CPSF3 cleavage enzyme (By similarity). Rescues cells from apoptosis by promoting activation of serine/threonine-protein kinase AKT1 through mRNA export of NBS1 which potentiates AKT1 phosphorylation and also through mRNA export of AKT1 effectors, allowing for increased production of these proteins (By similarity)"}],"commentType":"FUNCTION"},{"texts":[{"evidences":[{"evidenceCode":"ECO:0000250","source":"UniProtKB","id":"P63073"},{"evidenceCode":"ECO:0000269","source":"PubMed","id":"10856257"},{"evidenceCode":"ECO:0000269","source":"PubMed","id":"11408474"},{"evidenceCode":"ECO:0000269","source":"PubMed","id":"11500381"},{"evidenceCode":"ECO:0000269","source":"PubMed","id":"11575918"},{"evidenceCode":"ECO:0000269","source":"PubMed","id":"11879179"},{"evidenceCode":"ECO:0000269","source":"PubMed","id":"12554669"},{"evidenceCode":"ECO:0000269","source":"PubMed","id":"12897141"},{"evidenceCode":"ECO:0000269","source":"PubMed","id":"12975586"},{"evidenceCode":"ECO:0000269","source":"PubMed","id":"16157702"},{"evidenceCode":"ECO:0000269","source":"PubMed","id":"16271312"},{"evidenceCode":"ECO:0000269","source":"PubMed","id":"16699599"},{"evidenceCode":"ECO:0000269","source":"PubMed","id":"17631896"},{"evidenceCode":"ECO:0000269","source":"PubMed","id":"17667941"},{"evidenceCode":"ECO:0000269","source":"PubMed","id":"19262567"},{"evidenceCode":"ECO:0000269","source":"PubMed","id":"20430826"},{"evidenceCode":"ECO:0000269","source":"PubMed","id":"20616046"},{"evidenceCode":"ECO:0000269","source":"PubMed","id":"21661078"},{"evidenceCode":"ECO:0000269","source":"PubMed","id":"21883093"},{"evidenceCode":"ECO:0000269","source":"PubMed","id":"23814182"},{"evidenceCode":"ECO:0000269","source":"PubMed","id":"23991149"},{"evidenceCode":"ECO:0000269","source":"PubMed","id":"24207126"},{"evidenceCode":"ECO:0000269","source":"PubMed","id":"24335285"},{"evidenceCode":"ECO:0000269","source":"PubMed","id":"25533957"},{"evidenceCode":"ECO:0000269","source":"PubMed","id":"25702871"},{"evidenceCode":"ECO:0000269","source":"PubMed","id":"27117702"},{"evidenceCode":"ECO:0000269","source":"PubMed","id":"28325843"},{"evidenceCode":"ECO:0000269","source":"PubMed","id":"28487484"},{"evidenceCode":"ECO:0000269","source":"PubMed","id":"28733330"},{"evidenceCode":"ECO:0000269","source":"PubMed","id":"29358667"},{"evidenceCode":"ECO:0000269","source":"PubMed","id":"31042468"},{"evidenceCode":"ECO:0000269","source":"PubMed","id":"40441874"},{"evidenceCode":"ECO:0000269","source":"PubMed","id":"8521827"}],"value":"eIF4F is a multi-subunit complex, the composition of which varies with external and internal environmental conditions (PubMed:11408474, PubMed:11879179, PubMed:16271312, PubMed:17631896). It is composed of at least EIF4A, EIF4E and EIF4G1/EIF4G3 (PubMed:11408474, PubMed:11879179, PubMed:12975586, PubMed:29987188, PubMed:8521827). EIF4E is also known to interact with other partners (PubMed:11408474, PubMed:11879179, PubMed:12975586, PubMed:8521827). Interacts with EIF4ENIF1/4E-T; promotes recruitment to P-bodies and import into the nucleus (PubMed:10856257, PubMed:16157702, PubMed:23991149, PubMed:24335285, PubMed:28487484). Hypophosphorylated EIF4EBP1, EIF4EBP2 and EIF4EBP3 compete with EIF4G1/EIF4G3 to interact with EIF4E; insulin stimulated MAP-kinase (MAPK1 and MAPK3) phosphorylation of EIF4EBP1 causes dissociation of the complex allowing EIF4G1/EIF4G3 to bind and consequent initiation of translation (PubMed:16271312, PubMed:21661078, PubMed:24207126, PubMed:25533957, PubMed:25702871, PubMed:8521827). Interacts mutually exclusive with EIF4A1 or EIF4A2 (PubMed:11408474). Interacts with NGDN and PIWIL2 (By similarity). Component of the CYFIP1-EIF4E-FMR1 complex composed of CYFIP, EIF4E and FMR1 (By similarity). Interacts directly with CYFIP1 (By similarity). Interacts with CLOCK (By similarity). Binds to MKNK2 in nucleus (PubMed:12897141). Interacts with LIMD1, WTIP and AJUBA (PubMed:20616046). Interacts with APOBEC3G in an RNA-dependent manner (PubMed:16699599). Interacts with LARP1 (PubMed:20430826). Interacts with METTL3 (PubMed:27117702). Interacts with RBM24; this interaction prevents EIF4E from binding to p53/TP53 mRNA and inhibits the assembly of translation initiation complex (PubMed:29358667). Interacts with DDX3X; interaction is direct and in an RNA-independent manner; this interaction enhances EIF4E cap-binding ability and is required for the repression of cap-dependent translation and the increase of IRES-mediated translation (PubMed:17667941, PubMed:21883093, PubMed:28733330). DDX3X competes with EIF4G1 for interaction with EIF4E (PubMed:17667941, PubMed:21883093). Interacts with EIF4G1; which in a mutual exclusive interaction associates either with EIF1 or with EIF4E on a common binding site (PubMed:29987188). Interacts with BTG4 and CNOT7 (By similarity). Interacts with LRPPRC (via N-terminus); the interaction promotes association of EIF4E with 4ESE-containing mRNAs (PubMed:19262567, PubMed:28325843). Interacts with mRNA cleavage enzyme CPSF3 and its cofactor CPSF1 (PubMed:31042468). Interacts (via RING-type zinc finger) with PML; the interaction results in conformational changes of both interacting proteins and reduces EIF4E affinity for the 5' m7G cap of mRNA, thus reducing EIF4E-mediated mRNA nuclear export (PubMed:11500381, PubMed:11575918). Interacts with homeobox protein HHEX/PRH; the interaction inhibits EIF4E-mediated mRNA nuclear export (PubMed:12554669). Interacts with homeobox protein HOXA9; the interaction positively regulates EIF4E-mediated mRNA nuclear export (By similarity). Interacts with homeobox protein EMX2 (By similarity). Interacts with ANGEL1 (PubMed:40441874, PubMed:23814182)"}],"commentType":"SUBUNIT"},{"texts":[{"evidences":[{"evidenceCode":"ECO:0000269","source":"PubMed","id":"20212144"}],"value":"(Microbial infection) Interacts with Lassa virus Z protein"}],"commentType":"SUBUNIT"},{"texts":[{"evidences":[{"evidenceCode":"ECO:0000269","source":"PubMed","id":"11575918"}],"value":"(Microbial infection) Interacts with Lymphocytic choriomeningitis virus (LCMV) Z protein (via RING-type zinc finger); the interaction results in conformational changes of both interacting proteins and reduces EIF4E affinity for the m7G mRNA cap structure"}],"commentType":"SUBUNIT"},{"texts":[{"evidences":[{"evidenceCode":"ECO:0000269","source":"PubMed","id":"31712417"}],"value":"(Microbial infection) Interacts (via cap-binding region) with potato virus Y VPg; this interaction mediates the translation of the VPg-viral RNA conjugates and interferes with the cellular EIF4E-dependent mRNA export and translation"}],"commentType":"SUBUNIT"},{"commentType":"INTERACTION","interactions":[{"interactantOne":{"uniProtKBAccession":"P06730","intActId":"EBI-73440"},"interactantTwo":{"uniProtKBAccession":"O14965","geneName":"AURKA","intActId":"EBI-448680"},"numberOfExperiments":2,"organismDiffer":false},{"interactantOne":{"uniProtKBAccession":"P06730","intActId":"EBI-73440"},"interactantTwo":{"uniProtKBAccession":"Q13541","geneName":"EIF4EBP1","intActId":"EBI-74090"},"numberOfExperiments":34,"organismDiffer":false},{"interactantOne":{"uniProtKBAccession":"P06730","intActId":"EBI-73440"},"interactantTwo":{"uniProtKBAccession":"Q13542","geneName":"EIF4EBP2","intActId":"EBI-935137"},"numberOfExperiments":18,"organismDiffer":false},{"interactantOne":{"uniProtKBAccession":"P06730","intActId":"EBI-73440"},"interactantTwo":{"uniProtKBAccession":"O60516","geneName":"EIF4EBP3","intActId":"EBI-746950"},"numberOfExperiments":10,"organismDiffer":false},{"interactantOne":{"uniProtKBAccession":"P06730","intActId":"EBI-73440"},"interactantTwo":{"uniProtKBAccession":"Q9NRA8","geneName":"EIF4ENIF1","intActId":"EBI-301024"},"numberOfExperiments":15,"organismDiffer":false},{"interactantOne":{"uniProtKBAccession":"P06730","intActId":"EBI-73440"},"interactantTwo":{"uniProtKBAccession":"Q04637","geneName":"EIF4G1","intActId":"EBI-73711"},"numberOfExperiments":15,"organismDiffer":false},{"interactantOne":{"uniProtKBAccession":"P06730","intActId":"EBI-73440"},"interactantTwo":{"uniProtKBAccession":"O43432-1","geneName":"EIF4G3","intActId":"EBI-15841003"},"numberOfExperiments":2,"organismDiffer":false},{"interactantOne":{"uniProtKBAccession":"P06730","intActId":"EBI-73440"},"interactantTwo":{"uniProtKBAccession":"Q04743","geneName":"EMX2","intActId":"EBI-399831"},"numberOfExperiments":4,"organismDiffer":false},{"interactantOne":{"uniProtKBAccession":"P06730","intActId":"EBI-73440"},"interactantTwo":{"uniProtKBAccession":"Q8TEQ6","geneName":"GEMIN5","intActId":"EBI-443630"},"numberOfExperiments":3,"organismDiffer":false},{"interactantOne":{"uniProtKBAccession":"P06730","intActId":"EBI-73440"},"interactantTwo":{"uniProtKBAccession":"O15397","geneName":"IPO8","intActId":"EBI-358808"},"numberOfExperiments":2,"organismDiffer":false},{"interactantOne":{"uniProtKBAccession":"P06730","intActId":"EBI-73440"},"interactantTwo":{"uniProtKBAccession":"Q63ZY3","geneName":"KANK2","intActId":"EBI-2556193"},"numberOfExperiments":7,"organismDiffer":false},{"interactantOne":{"uniProtKBAccession":"P06730","intActId":"EBI-73440"},"interactantTwo":{"uniProtKBAccession":"P42704","geneName":"LRPPRC","intActId":"EBI-1050853"},"numberOfExperiments":6,"organismDiffer":false},{"interactantOne":{"uniProtKBAccession":"P06730","intActId":"EBI-73440"},"interactantTwo":{"uniProtKBAccession":"P11940","geneName":"PABPC1","intActId":"EBI-81531"},"numberOfExperiments":5,"organismDiffer":false},{"interactantOne":{"uniProtKBAccession":"P06730","intActId":"EBI-73440"},"interactantTwo":{"uniProtKBAccession":"P29590","geneName":"PML","intActId":"EBI-295890"},"numberOfExperiments":5,"organismDiffer":false},{"interactantOne":{"uniProtKBAccession":"P06730","intActId":"EBI-73440"},"interactantTwo":{"uniProtKBAccession":"P67775","geneName":"PPP2CA","intActId":"EBI-712311"},"numberOfExperiments":2,"organismDiffer":false},{"interactantOne":{"uniProtKBAccession":"P06730","intActId":"EBI-73440"},"interactantTwo":{"uniProtKBAccession":"O43148","geneName":"RNMT","intActId":"EBI-877832"},"numberOfExperiments":8,"organismDiffer":false},{"interactantOne":{"uniProtKBAccession":"P06730","intActId":"EBI-73440"},"interactantTwo":{"uniProtKBAccession":"P63165","geneName":"SUMO1","intActId":"EBI-80140"},"numberOfExperiments":5,"organismDiffer":false},{"interactantOne":{"uniProtKBAccession":"P06730","intActId":"EBI-73440"},"interactantTwo":{"uniProtKBAccession":"P48775","geneName":"TDO2","intActId":"EBI-743494"},"numberOfExperiments":4,"organismDiffer":false},{"interactantOne":{"uniProtKBAccession":"P06730","intActId":"EBI-73440"},"interactantTwo":{"uniProtKBAccession":"P14373","geneName":"TRIM27","intActId":"EBI-719493"},"numberOfExperiments":5,"organismDiffer":false},{"interactantOne":{"uniProtKBAccession":"P06730","intActId":"EBI-73440"},"interactantTwo":{"uniProtKBAccession":"Q5T124","geneName":"UBXN11","intActId":"EBI-746004"},"numberOfExperiments":3,"organismDiffer":false},{"interactantOne":{"uniProtKBAccession":"P06730","intActId":"EBI-73440"},"interactantTwo":{"uniProtKBAccession":"O70552","geneName":"Btg4","intActId":"EBI-16204405"},"numberOfExperiments":4,"organismDiffer":true},{"interactantOne":{"uniProtKBAccession":"P06730","intActId":"EBI-73440"},"interactantTwo":{"uniProtKBAccession":"Q60809","geneName":"Cnot7","intActId":"EBI-2104739"},"numberOfExperiments":2,"organismDiffer":true},{"interactantOne":{"uniProtKBAccession":"P06730","intActId":"EBI-73440"},"interactantTwo":{"uniProtKBAccession":"Q60953","geneName":"Pml","intActId":"EBI-3895605"},"numberOfExperiments":4,"organismDiffer":true},{"interactantOne":{"uniProtKBAccession":"P06730","intActId":"EBI-73440"},"interactantTwo":{"uniProtKBAccession":"O73557","geneName":"Z","intActId":"EBI-15840965"},"numberOfExperiments":3,"organismDiffer":true},{"interactantOne":{"uniProtKBAccession":"P06730","intActId":"EBI-73440"},"interactantTwo":{"uniProtKBAccession":"P18541","geneName":"Z","intActId":"EBI-15954802"},"numberOfExperiments":4,"organismDiffer":true},{"interactantOne":{"uniProtKBAccession":"P06730","intActId":"EBI-73440"},"interactantTwo":{"uniProtKBAccession":"P18247","intActId":"EBI-66896638"},"numberOfExperiments":6,"organismDiffer":true},{"interactantOne":{"uniProtKBAccession":"P06730-1","intActId":"EBI-32715456"},"interactantTwo":{"uniProtKBAccession":"Q13541","geneName":"EIF4EBP1","intActId":"EBI-74090"},"numberOfExperiments":3,"organismDiffer":false},{"interactantOne":{"uniProtKBAccession":"P06730-1","intActId":"EBI-32715456"},"interactantTwo":{"uniProtKBAccession":"Q9NRA8","geneName":"EIF4ENIF1","intActId":"EBI-301024"},"numberOfExperiments":2,"organismDiffer":false}]},{"commentType":"SUBCELLULAR LOCATION","note":{"texts":[{"evidences":[{"evidenceCode":"ECO:0000250","source":"UniProtKB","id":"P63073"},{"evidenceCode":"ECO:0000269","source":"PubMed","id":"10856257"},{"evidenceCode":"ECO:0000269","source":"PubMed","id":"16157702"},{"evidenceCode":"ECO:0000269","source":"PubMed","id":"24335285"},{"evidenceCode":"ECO:0000269","source":"PubMed","id":"25923732"}],"value":"Interaction with EIF4ENIF1/4E-T is required for localization to processing bodies (P-bodies) (PubMed:16157702, PubMed:24335285, PubMed:25923732). Imported in the nucleus via interaction with EIF4ENIF1/4E-T via a piggy-back mechanism (PubMed:10856257). Sequestered in the nucleus by EIF4EBP1 and EIF4EBP2 (By similarity)"}]},"subcellularLocations":[{"location":{"evidences":[{"evidenceCode":"ECO:0000269","source":"PubMed","id":"16157702"},{"evidenceCode":"ECO:0000269","source":"PubMed","id":"20616046"},{"evidenceCode":"ECO:0000269","source":"PubMed","id":"24335285"},{"evidenceCode":"ECO:0000269","source":"PubMed","id":"25923732"}],"value":"Cytoplasm, P-body","id":"SL-0230"}},{"location":{"evidences":[{"evidenceCode":"ECO:0000269","source":"PubMed","id":"10856257"},{"evidenceCode":"ECO:0000269","source":"PubMed","id":"12554669"},{"evidenceCode":"ECO:0000269","source":"PubMed","id":"1384058"},{"evidenceCode":"ECO:0000269","source":"PubMed","id":"15657436"},{"evidenceCode":"ECO:0000269","source":"PubMed","id":"21883093"},{"evidenceCode":"ECO:0000269","source":"PubMed","id":"23471078"},{"evidenceCode":"ECO:0000269","source":"PubMed","id":"36843541"}],"value":"Cytoplasm","id":"SL-0086"}},{"location":{"evidences":[{"evidenceCode":"ECO:0000269","source":"PubMed","id":"21883093"}],"value":"Cytoplasm, Stress granule","id":"SL-0496"}},{"location":{"evidences":[{"evidenceCode":"ECO:0000269","source":"PubMed","id":"10856257"},{"evidenceCode":"ECO:0000269","source":"PubMed","id":"11423616"},{"evidenceCode":"ECO:0000269","source":"PubMed","id":"1384058"},{"evidenceCode":"ECO:0000269","source":"PubMed","id":"23471078"},{"evidenceCode":"ECO:0000269","source":"PubMed","id":"36843541"}],"value":"Nucleus","id":"SL-0191"}},{"location":{"evidences":[{"evidenceCode":"ECO:0000269","source":"PubMed","id":"10648556"}],"value":"Nucleus speckle","id":"SL-0186"}},{"location":{"evidences":[{"evidenceCode":"ECO:0000269","source":"PubMed","id":"12554669"},{"evidenceCode":"ECO:0000269","source":"PubMed","id":"15657436"}],"value":"Nucleus, nuclear body","id":"SL-0494"}}]},{"commentType":"ALTERNATIVE PRODUCTS","events":["Alternative splicing"],"isoforms":[{"name":{"value":"1"},"isoformIds":["P06730-1"],"isoformSequenceStatus":"Displayed"},{"name":{"value":"2"},"isoformIds":["P06730-2"],"sequenceIds":["VSP_042014"],"isoformSequenceStatus":"Described"},{"name":{"value":"3"},"isoformIds":["P06730-3"],"sequenceIds":["VSP_043591"],"isoformSequenceStatus":"Described"}]},{"texts":[{"evidences":[{"evidenceCode":"ECO:0000250","source":"UniProtKB","id":"P63073"},{"evidenceCode":"ECO:0000269","source":"PubMed","id":"11154262"},{"evidenceCode":"ECO:0000269","source":"PubMed","id":"11606200"},{"evidenceCode":"ECO:0000269","source":"PubMed","id":"12138083"},{"evidenceCode":"ECO:0000269","source":"PubMed","id":"3112145"},{"evidenceCode":"ECO:0000269","source":"PubMed","id":"7590282"},{"evidenceCode":"ECO:0000269","source":"PubMed","id":"7782323"},{"evidenceCode":"ECO:0000269","source":"PubMed","id":"8505316"},{"evidenceCode":"ECO:0000269","source":"PubMed","id":"9878069"}],"value":"Phosphorylation increases the ability of the protein to bind to mRNA caps and to form the eIF4F complex (PubMed:11154262, PubMed:3112145, PubMed:7590282, PubMed:7782323, PubMed:8505316, PubMed:9878069). Phosphorylation also enhances its mRNA transport function (By similarity). Phosphorylation at Ser-209 is not essential for protein synthesis (PubMed:11606200, PubMed:12138083)"}],"commentType":"PTM"},{"commentType":"MASS SPECTROMETRY","method":"Electrospray","molWeight":24964.3,"molWeightError":0.0,"evidences":[{"evidenceCode":"ECO:0000269","source":"PubMed","id":"17036047"}]},{"commentType":"MASS SPECTROMETRY","method":"Electrospray","molWeight":24960.0,"molWeightError":0.0,"evidences":[{"evidenceCode":"ECO:0000269","source":"PubMed","id":"17631896"}]},{"commentType":"DISEASE","disease":{"diseaseId":"Autism 19","diseaseAccession":"DI-03649","acronym":"AUTS19","description":"A complex multifactorial, pervasive developmental disorder characterized by impairments in reciprocal social interaction and communication, restricted and stereotyped patterns of interests and activities, and the presence of developmental abnormalities by 3 years of age. Most individuals with autism also manifest moderate intellectual disability.","diseaseCrossReference":{"database":"MIM","id":"615091"},"evidences":[{"evidenceCode":"ECO:0000269","source":"PubMed","id":"19556253"}]},"note":{"texts":[{"evidences":[{"evidenceCode":"ECO:0000269","source":"PubMed","id":"19556253"}],"value":"Disease susceptibility is associated with variants affecting the gene represented in this entry. A heterozygous single-nucleotide insertion has been found in families affected by autism. The variant results in increased promoter activity and is involved in disease pathogenesis through EIF4E deregulation (PubMed:19556253)"}]}},{"commentType":"DISEASE","note":{"texts":[{"evidences":[{"evidenceCode":"ECO:0000269","source":"PubMed","id":"19556253"}],"value":"A chromosomal aberration involving EIF4E has been found in a patient with classic autism. Translocation t(45)(q23q31.3). The breakpoint on chromosome 4 is located 56 kb downstream of EIF4E (PubMed:19556253)"}]}},{"texts":[{"evidences":[{"evidenceCode":"ECO:0000269","source":"PubMed","id":"15601771"},{"evidenceCode":"ECO:0000269","source":"PubMed","id":"19433856"}],"value":"The antiviral drug ribavirin relocalizes nuclear EIF4E to the cytoplasm and reduces the elevated EIF4E levels found in acute myeloid leukemia patients, suggesting its potential use as a therapeutic agent (PubMed:19433856). Ribavirin suppresses EIF4E-mediated oncogenic transformation by binding to EIF4E at the functional site used by the m7G mRNA cap and competing with the mRNA cap for binding to EIF4E which leads to relocalization of the majority of EIF4E to the cytoplasm and inhibition of nucleocytoplasmic mRNA transport (PubMed:15601771)"}],"commentType":"MISCELLANEOUS"},{"texts":[{"evidences":[{"evidenceCode":"ECO:0000305"}],"value":"Belongs to the eukaryotic initiation factor 4E family"}],"commentType":"SIMILARITY"},{"texts":[{"evidences":[{"evidenceCode":"ECO:0000250","source":"UniProtKB","id":"A0A9J7FAT4"},{"evidenceCode":"ECO:0000269","source":"PubMed","id":"3112145"}],"value":"Was originally thought to be phosphorylated on Ser-53 (PubMed:3112145). 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