4ET_HUMAN
ID 4ET_HUMAN Reviewed; 985 AA.
AC Q9NRA8; B1AKL2; B1AKL3; B2RBF1; Q8NCF2; Q9H708;
DT 02-AUG-2002, integrated into UniProtKB/Swiss-Prot.
DT 02-AUG-2002, sequence version 2.
DT 03-AUG-2022, entry version 184.
DE RecName: Full=Eukaryotic translation initiation factor 4E transporter {ECO:0000303|PubMed:10856257};
DE Short=4E-T {ECO:0000303|PubMed:10856257};
DE Short=eIF4E transporter {ECO:0000303|PubMed:10856257};
DE AltName: Full=Eukaryotic translation initiation factor 4E nuclear import factor 1;
GN Name=EIF4ENIF1 {ECO:0000312|HGNC:HGNC:16687};
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]
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), FUNCTION, SUBCELLULAR LOCATION,
RP PHOSPHORYLATION, TISSUE SPECIFICITY, AND MUTAGENESIS OF TYR-30 AND
RP 195-ARG-ARG-196.
RC TISSUE=Fetal brain;
RX PubMed=10856257; DOI=10.1093/emboj/19.12.3142;
RA Dostie J., Ferraiuolo M., Pause A., Adam S.A., Sonenberg N.;
RT "A novel shuttling protein, 4E-T, mediates the nuclear import of the mRNA
RT 5' cap-binding protein, eIF4E.";
RL EMBO J. 19:3142-3156(2000).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
RX PubMed=15461802; DOI=10.1186/gb-2004-5-10-r84;
RA Collins J.E., Wright C.L., Edwards C.A., Davis M.P., Grinham J.A.,
RA Cole C.G., Goward M.E., Aguado B., Mallya M., Mokrab Y., Huckle E.J.,
RA Beare D.M., Dunham I.;
RT "A genome annotation-driven approach to cloning the human ORFeome.";
RL Genome Biol. 5:R84.1-R84.11(2004).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 3).
RC TISSUE=Colon, Placenta, and Teratocarcinoma;
RX PubMed=14702039; DOI=10.1038/ng1285;
RA Ota T., Suzuki Y., Nishikawa T., Otsuki T., Sugiyama T., Irie R.,
RA Wakamatsu A., Hayashi K., Sato H., Nagai K., Kimura K., Makita H.,
RA Sekine M., Obayashi M., Nishi T., Shibahara T., Tanaka T., Ishii S.,
RA Yamamoto J., Saito K., Kawai Y., Isono Y., Nakamura Y., Nagahari K.,
RA Murakami K., Yasuda T., Iwayanagi T., Wagatsuma M., Shiratori A., Sudo H.,
RA Hosoiri T., Kaku Y., Kodaira H., Kondo H., Sugawara M., Takahashi M.,
RA Kanda K., Yokoi T., Furuya T., Kikkawa E., Omura Y., Abe K., Kamihara K.,
RA Katsuta N., Sato K., Tanikawa M., Yamazaki M., Ninomiya K., Ishibashi T.,
RA Yamashita H., Murakawa K., Fujimori K., Tanai H., Kimata M., Watanabe M.,
RA Hiraoka S., Chiba Y., Ishida S., Ono Y., Takiguchi S., Watanabe S.,
RA Yosida M., Hotuta T., Kusano J., Kanehori K., Takahashi-Fujii A., Hara H.,
RA Tanase T.-O., Nomura Y., Togiya S., Komai F., Hara R., Takeuchi K.,
RA Arita M., Imose N., Musashino K., Yuuki H., Oshima A., Sasaki N.,
RA Aotsuka S., Yoshikawa Y., Matsunawa H., Ichihara T., Shiohata N., Sano S.,
RA Moriya S., Momiyama H., Satoh N., Takami S., Terashima Y., Suzuki O.,
RA Nakagawa S., Senoh A., Mizoguchi H., Goto Y., Shimizu F., Wakebe H.,
RA Hishigaki H., Watanabe T., Sugiyama A., Takemoto M., Kawakami B.,
RA Yamazaki M., Watanabe K., Kumagai A., Itakura S., Fukuzumi Y., Fujimori Y.,
RA Komiyama M., Tashiro H., Tanigami A., Fujiwara T., Ono T., Yamada K.,
RA Fujii Y., Ozaki K., Hirao M., Ohmori Y., Kawabata A., Hikiji T.,
RA Kobatake N., Inagaki H., Ikema Y., Okamoto S., Okitani R., Kawakami T.,
RA Noguchi S., Itoh T., Shigeta K., Senba T., Matsumura K., Nakajima Y.,
RA Mizuno T., Morinaga M., Sasaki M., Togashi T., Oyama M., Hata H.,
RA Watanabe M., Komatsu T., Mizushima-Sugano J., Satoh T., Shirai Y.,
RA Takahashi Y., Nakagawa K., Okumura K., Nagase T., Nomura N., Kikuchi H.,
RA Masuho Y., Yamashita R., Nakai K., Yada T., Nakamura Y., Ohara O.,
RA Isogai T., Sugano S.;
RT "Complete sequencing and characterization of 21,243 full-length human
RT cDNAs.";
RL Nat. Genet. 36:40-45(2004).
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=10591208; DOI=10.1038/990031;
RA Dunham I., Hunt A.R., Collins J.E., Bruskiewich R., Beare D.M., Clamp M.,
RA Smink L.J., Ainscough R., Almeida J.P., Babbage A.K., Bagguley C.,
RA Bailey J., Barlow K.F., Bates K.N., Beasley O.P., Bird C.P., Blakey S.E.,
RA Bridgeman A.M., Buck D., Burgess J., Burrill W.D., Burton J., Carder C.,
RA Carter N.P., Chen Y., Clark G., Clegg S.M., Cobley V.E., Cole C.G.,
RA Collier R.E., Connor R., Conroy D., Corby N.R., Coville G.J., Cox A.V.,
RA Davis J., Dawson E., Dhami P.D., Dockree C., Dodsworth S.J., Durbin R.M.,
RA Ellington A.G., Evans K.L., Fey J.M., Fleming K., French L., Garner A.A.,
RA Gilbert J.G.R., Goward M.E., Grafham D.V., Griffiths M.N.D., Hall C.,
RA Hall R.E., Hall-Tamlyn G., Heathcott R.W., Ho S., Holmes S., Hunt S.E.,
RA Jones M.C., Kershaw J., Kimberley A.M., King A., Laird G.K., Langford C.F.,
RA Leversha M.A., Lloyd C., Lloyd D.M., Martyn I.D., Mashreghi-Mohammadi M.,
RA Matthews L.H., Mccann O.T., Mcclay J., Mclaren S., McMurray A.A.,
RA Milne S.A., Mortimore B.J., Odell C.N., Pavitt R., Pearce A.V., Pearson D.,
RA Phillimore B.J.C.T., Phillips S.H., Plumb R.W., Ramsay H., Ramsey Y.,
RA Rogers L., Ross M.T., Scott C.E., Sehra H.K., Skuce C.D., Smalley S.,
RA Smith M.L., Soderlund C., Spragon L., Steward C.A., Sulston J.E.,
RA Swann R.M., Vaudin M., Wall M., Wallis J.M., Whiteley M.N., Willey D.L.,
RA Williams L., Williams S.A., Williamson H., Wilmer T.E., Wilming L.,
RA Wright C.L., Hubbard T., Bentley D.R., Beck S., Rogers J., Shimizu N.,
RA Minoshima S., Kawasaki K., Sasaki T., Asakawa S., Kudoh J., Shintani A.,
RA Shibuya K., Yoshizaki Y., Aoki N., Mitsuyama S., Roe B.A., Chen F., Chu L.,
RA Crabtree J., Deschamps S., Do A., Do T., Dorman A., Fang F., Fu Y., Hu P.,
RA Hua A., Kenton S., Lai H., Lao H.I., Lewis J., Lewis S., Lin S.-P., Loh P.,
RA Malaj E., Nguyen T., Pan H., Phan S., Qi S., Qian Y., Ray L., Ren Q.,
RA Shaull S., Sloan D., Song L., Wang Q., Wang Y., Wang Z., White J.,
RA Willingham D., Wu H., Yao Z., Zhan M., Zhang G., Chissoe S., Murray J.,
RA Miller N., Minx P., Fulton R., Johnson D., Bemis G., Bentley D.,
RA Bradshaw H., Bourne S., Cordes M., Du Z., Fulton L., Goela D., Graves T.,
RA Hawkins J., Hinds K., Kemp K., Latreille P., Layman D., Ozersky P.,
RA Rohlfing T., Scheet P., Walker C., Wamsley A., Wohldmann P., Pepin K.,
RA Nelson J., Korf I., Bedell J.A., Hillier L.W., Mardis E., Waterston R.,
RA Wilson R., Emanuel B.S., Shaikh T., Kurahashi H., Saitta S., Budarf M.L.,
RA McDermid H.E., Johnson A., Wong A.C.C., Morrow B.E., Edelmann L., Kim U.J.,
RA Shizuya H., Simon M.I., Dumanski J.P., Peyrard M., Kedra D., Seroussi E.,
RA Fransson I., Tapia I., Bruder C.E., O'Brien K.P., Wilkinson P.,
RA Bodenteich A., Hartman K., Hu X., Khan A.S., Lane L., Tilahun Y.,
RA Wright H.;
RT "The DNA sequence of human chromosome 22.";
RL Nature 402:489-495(1999).
RN [5]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RA Mural R.J., Istrail S., Sutton G.G., Florea L., Halpern A.L., Mobarry C.M.,
RA Lippert R., Walenz B., Shatkay H., Dew I., Miller J.R., Flanigan M.J.,
RA Edwards N.J., Bolanos R., Fasulo D., Halldorsson B.V., Hannenhalli S.,
RA Turner R., Yooseph S., Lu F., Nusskern D.R., Shue B.C., Zheng X.H.,
RA Zhong F., Delcher A.L., Huson D.H., Kravitz S.A., Mouchard L., Reinert K.,
RA Remington K.A., Clark A.G., Waterman M.S., Eichler E.E., Adams M.D.,
RA Hunkapiller M.W., Myers E.W., Venter J.C.;
RL Submitted (JUL-2005) to the EMBL/GenBank/DDBJ databases.
RN [6]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 1 AND 2).
RC TISSUE=Testis;
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]
RP FUNCTION, SUBCELLULAR LOCATION, INTERACTION WITH EIF4E, DOMAIN, AND
RP MUTAGENESIS OF TYR-30.
RX PubMed=16157702; DOI=10.1083/jcb.200504039;
RA Ferraiuolo M.A., Basak S., Dostie J., Murray E.L., Schoenberg D.R.,
RA Sonenberg N.;
RT "A role for the eIF4E-binding protein 4E-T in P-body formation and mRNA
RT decay.";
RL J. Cell Biol. 170:913-924(2005).
RN [8]
RP INTERACTION WITH APOBEC3G.
RX PubMed=16699599; DOI=10.1371/journal.ppat.0020041;
RA Wichroski M.J., Robb G.B., Rana T.M.;
RT "Human retroviral host restriction factors APOBEC3G and APOBEC3F localize
RT to mRNA processing bodies.";
RL PLoS Pathog. 2:E41-E41(2006).
RN [9]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-920, AND IDENTIFICATION BY
RP 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 [10]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-120; SER-136; SER-138;
RP SER-345; SER-564 AND SER-951, AND IDENTIFICATION BY MASS SPECTROMETRY
RP [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 [11]
RP IDENTIFICATION BY MASS 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 [12]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-5; SER-564; SER-587 AND
RP SER-693, AND IDENTIFICATION BY 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 [13]
RP ACETYLATION [LARGE SCALE ANALYSIS] AT LYS-486, AND IDENTIFICATION BY MASS
RP SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=19608861; DOI=10.1126/science.1175371;
RA Choudhary C., Kumar C., Gnad F., Nielsen M.L., Rehman M., Walther T.C.,
RA Olsen J.V., Mann M.;
RT "Lysine acetylation targets protein complexes and co-regulates major
RT cellular functions.";
RL Science 325:834-840(2009).
RN [14]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-5; SER-301; SER-513; SER-564
RP AND SER-951, AND IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE
RP 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 [15]
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 [16]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-951, 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 [17]
RP SUBCELLULAR LOCATION.
RX PubMed=22090346; DOI=10.1091/mbc.e11-05-0415;
RA Marnef A., Weil D., Standart N.;
RT "RNA-related nuclear functions of human Pat1b, the P-body mRNA decay
RT factor.";
RL Mol. Biol. Cell 23:213-224(2012).
RN [18]
RP FUNCTION, SUBCELLULAR LOCATION, PHOSPHORYLATION AT SER-301; SER-374;
RP SER-513; SER-587; SER-693 AND SER-752, AND MUTAGENESIS OF SER-301; SER-374;
RP SER-513; SER-587; SER-693 AND SER-752.
RX PubMed=22966201; DOI=10.1128/mcb.00544-12;
RA Cargnello M., Tcherkezian J., Dorn J.F., Huttlin E.L., Maddox P.S.,
RA Gygi S.P., Roux P.P.;
RT "Phosphorylation of the eukaryotic translation initiation factor 4E-
RT transporter (4E-T) by c-Jun N-terminal kinase promotes stress-dependent P-
RT body assembly.";
RL Mol. Cell. Biol. 32:4572-4584(2012).
RN [19]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-5; SER-74; SER-78; SER-115;
RP SER-417; SER-513; SER-564; SER-587 AND SER-951, AND IDENTIFICATION BY MASS
RP 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 [20]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-353 AND SER-951, AND
RP IDENTIFICATION BY 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 [21]
RP SUBCELLULAR LOCATION, INTERACTION WITH EIF4E AND EIF4E2, DOMAIN, AND
RP MUTAGENESIS OF 30-TYR--LEU-36; TYR-30; 35-LEU-LEU-36 AND 54-LYS--TRP-61.
RX PubMed=23991149; DOI=10.1371/journal.pone.0072761;
RA Kubacka D., Kamenska A., Broomhead H., Minshall N., Darzynkiewicz E.,
RA Standart N.;
RT "Investigating the consequences of eIF4E2 (4EHP) interaction with 4E-
RT transporter on its cellular distribution in HeLa cells.";
RL PLoS ONE 8:e72761-e72761(2013).
RN [22]
RP FUNCTION, SUBCELLULAR LOCATION, INTERACTION WITH EIF4E, DOMAIN, AND
RP MUTAGENESIS OF TYR-30.
RX PubMed=24335285; DOI=10.1093/nar/gkt1265;
RA Kamenska A., Lu W.T., Kubacka D., Broomhead H., Minshall N., Bushell M.,
RA Standart N.;
RT "Human 4E-T represses translation of bound mRNAs and enhances microRNA-
RT mediated silencing.";
RL Nucleic Acids Res. 42:3298-3313(2014).
RN [23]
RP INTERACTION WITH DDX6; CNOT1; PATL1 AND LSM14A.
RX PubMed=26027925; DOI=10.1016/j.celrep.2015.04.065;
RA Nishimura T., Padamsi Z., Fakim H., Milette S., Dunham W.H., Gingras A.C.,
RA Fabian M.R.;
RT "The eIF4E-Binding protein 4E-T is a component of the mRNA decay machinery
RT that bridges the 5' and 3' termini of target mRNAs.";
RL Cell Rep. 11:1425-1436(2015).
RN [24]
RP INTERACTION WITH EIF4E.
RX PubMed=25923732; DOI=10.1371/journal.pone.0123352;
RA Martinez A., Sese M., Losa J.H., Robichaud N., Sonenberg N., Aasen T.,
RA Ramon Y Cajal S.;
RT "Phosphorylation of eIF4E confers resistance to cellular stress and DNA-
RT damaging agents through an interaction with 4E-T: a rationale for novel
RT therapeutic approaches.";
RL PLoS ONE 10:e0123352-e0123352(2015).
RN [25]
RP FUNCTION, DOMAIN, AND INTERACTION WITH DDX6; CSDE1 AND CNOT1.
RX PubMed=27342281; DOI=10.1093/nar/gkw565;
RA Kamenska A., Simpson C., Vindry C., Broomhead H., Benard M.,
RA Ernoult-Lange M., Lee B.P., Harries L.W., Weil D., Standart N.;
RT "The DDX6-4E-T interaction mediates translational repression and P-body
RT assembly.";
RL Nucleic Acids Res. 44:6318-6334(2016).
RN [26]
RP SUMOYLATION [LARGE SCALE ANALYSIS] AT LYS-410, 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).
RN [27]
RP FUNCTION, INTERACTION WITH EIF4E AND EIF4E2, AND MUTAGENESIS OF
RP 30-TYR--LEU-36 AND TYR-30.
RX PubMed=28487484; DOI=10.1073/pnas.1701488114;
RA Chapat C., Jafarnejad S.M., Matta-Camacho E., Hesketh G.G., Gelbart I.A.,
RA Attig J., Gkogkas C.G., Alain T., Stern-Ginossar N., Fabian M.R.,
RA Gingras A.C., Duchaine T.F., Sonenberg N.;
RT "Cap-binding protein 4EHP effects translation silencing by microRNAs.";
RL Proc. Natl. Acad. Sci. U.S.A. 114:5425-5430(2017).
RN [28]
RP FUNCTION, SUBCELLULAR LOCATION, AND INTERACTION WITH DDX6.
RX PubMed=28216671; DOI=10.1038/srep42853;
RA Huang J.H., Ku W.C., Chen Y.C., Chang Y.L., Chu C.Y.;
RT "Dual mechanisms regulate the nucleocytoplasmic localization of human
RT DDX6.";
RL Sci. Rep. 7:42853-42853(2017).
RN [29]
RP INTERACTION WITH DDX6.
RX PubMed=31422817; DOI=10.1016/j.ajhg.2019.07.010;
RA Balak C., Benard M., Schaefer E., Iqbal S., Ramsey K., Ernoult-Lange M.,
RA Mattioli F., Llaci L., Geoffroy V., Courel M., Naymik M., Bachman K.K.,
RA Pfundt R., Rump P., Ter Beest J., Wentzensen I.M., Monaghan K.G.,
RA McWalter K., Richholt R., Le Bechec A., Jepsen W., De Both M., Belnap N.,
RA Boland A., Piras I.S., Deleuze J.F., Szelinger S., Dollfus H., Chelly J.,
RA Muller J., Campbell A., Lal D., Rangasamy S., Mandel J.L., Narayanan V.,
RA Huentelman M., Weil D., Piton A.;
RT "Rare de novo missense variants in RNA helicase DDX6 cause intellectual
RT disability and dysmorphic features and lead to P-body defects and RNA
RT dysregulation.";
RL Am. J. Hum. Genet. 105:509-525(2019).
RN [30]
RP INTERACTION WITH DDX6.
RX PubMed=31439631; DOI=10.1101/gad.329219.119;
RA Peter D., Ruscica V., Bawankar P., Weber R., Helms S., Valkov E.,
RA Igreja C., Izaurralde E.;
RT "Molecular basis for GIGYF-Me31B complex assembly in 4EHP-mediated
RT translational repression.";
RL Genes Dev. 33:1355-1360(2019).
RN [31]
RP FUNCTION, SUBCELLULAR LOCATION, AND INTERACTION WITH CSDE1; DDX6; CNOT1;
RP PATL1 AND LSM14A.
RX PubMed=32354837; DOI=10.1101/gad.336073.119;
RA Raesch F., Weber R., Izaurralde E., Igreja C.;
RT "4E-T-bound mRNAs are stored in a silenced and deadenylated form.";
RL Genes Dev. 34:847-860(2020).
RN [32] {ECO:0007744|PDB:5ANR}
RP X-RAY CRYSTALLOGRAPHY (2.10 ANGSTROMS) OF 199-239 IN COMPLEX WITH DDX6 AND
RP CNOT1, AND INTERACTION WITH DDX6 AND CNOT1.
RX PubMed=26489469; DOI=10.1016/j.celrep.2015.09.033;
RA Ozgur S., Basquin J., Kamenska A., Filipowicz W., Standart N., Conti E.;
RT "Structure of a human 4E-T/DDX6/CNOT1 complex reveals the different
RT interplay of DDX6-binding proteins with the CCR4-NOT complex.";
RL Cell Rep. 13:703-711(2015).
RN [33] {ECO:0007744|PDB:6F9W}
RP X-RAY CRYSTALLOGRAPHY (2.62 ANGSTROMS) OF 954-985 IN COMPLEX WITH LSM14A,
RP INTERACTION WITH LSM14A, AND MUTAGENESIS OF 955-LEU--TRP-958; TRP-958;
RP PHE-959; SER-961; SER-970; 978-VAL--LEU-981; VAL-978 AND GLU-982.
RX PubMed=29510985; DOI=10.15252/embj.201797869;
RA Brandmann T., Fakim H., Padamsi Z., Youn J.Y., Gingras A.C., Fabian M.R.,
RA Jinek M.;
RT "Molecular architecture of LSM14 interactions involved in the assembly of
RT mRNA silencing complexes.";
RL EMBO J. 37:0-0(2018).
CC -!- FUNCTION: EIF4E-binding protein that regulates translation and
CC stability of mRNAs in processing bodies (P-bodies) (PubMed:16157702,
CC PubMed:24335285, PubMed:27342281, PubMed:32354837). Plays a key role in
CC P-bodies to coordinate the storage of translationally inactive mRNAs in
CC the cytoplasm and prevent their degradation (PubMed:24335285,
CC PubMed:32354837). Acts as a binding platform for multiple RNA-binding
CC proteins: promotes deadenylation of mRNAs via its interaction with the
CC CCR4-NOT complex, and blocks decapping via interaction with eIF4E
CC (EIF4E and EIF4E2), thereby protecting deadenylated and repressed mRNAs
CC from degradation (PubMed:27342281, PubMed:32354837). Component of a
CC multiprotein complex that sequesters and represses translation of
CC proneurogenic factors during neurogenesis (By similarity). Promotes
CC miRNA-mediated translational repression (PubMed:24335285,
CC PubMed:27342281, PubMed:28487484). Required for the formation of P-
CC bodies (PubMed:16157702, PubMed:22966201, PubMed:27342281,
CC PubMed:32354837). Involved in mRNA translational repression mediated by
CC the miRNA effector TNRC6B by protecting TNRC6B-targeted mRNAs from
CC decapping and subsequent decay (PubMed:32354837). Also acts as a
CC nucleoplasmic shuttling protein, which mediates the nuclear import of
CC EIF4E and DDX6 by a piggy-back mechanism (PubMed:10856257,
CC PubMed:28216671). {ECO:0000250|UniProtKB:Q9EST3,
CC ECO:0000269|PubMed:10856257, ECO:0000269|PubMed:16157702,
CC ECO:0000269|PubMed:22966201, ECO:0000269|PubMed:24335285,
CC ECO:0000269|PubMed:27342281, ECO:0000269|PubMed:28216671,
CC ECO:0000269|PubMed:28487484, ECO:0000269|PubMed:32354837}.
CC -!- SUBUNIT: Interacts (via YXXXXLphi motif) with EIF4E (PubMed:10856257,
CC PubMed:16157702, PubMed:23991149, PubMed:24335285, PubMed:25923732,
CC PubMed:28487484). Interacts (via YXXXXLphi motif) with EIF4E2
CC (PubMed:23991149, PubMed:28487484). Interacts with DDX6
CC (PubMed:26027925, PubMed:27342281, PubMed:28216671, PubMed:31422817,
CC PubMed:32354837, PubMed:26489469, PubMed:31439631). Interacts with
CC CSDE1/UNR (PubMed:27342281, PubMed:32354837). Interacts with CNOT1;
CC promoting association with the CCR4-NOT complex (PubMed:26027925,
CC PubMed:27342281, PubMed:32354837, PubMed:26489469). Interacts with
CC LSM14A; promoting EIF4ENIF1 localization to P-bodies (PubMed:26027925,
CC PubMed:32354837, PubMed:29510985). Interacts with PATL1
CC (PubMed:26027925, PubMed:32354837). Interacts with importin beta only
CC in the presence of importin alpha, suggesting a direct interaction with
CC importin alpha (PubMed:10856257). Interacts with APOBEC3G in an RNA-
CC dependent manner (PubMed:16699599). {ECO:0000269|PubMed:10856257,
CC ECO:0000269|PubMed:16157702, ECO:0000269|PubMed:16699599,
CC ECO:0000269|PubMed:23991149, ECO:0000269|PubMed:24335285,
CC ECO:0000269|PubMed:25923732, ECO:0000269|PubMed:26027925,
CC ECO:0000269|PubMed:26489469, ECO:0000269|PubMed:27342281,
CC ECO:0000269|PubMed:28216671, ECO:0000269|PubMed:28487484,
CC ECO:0000269|PubMed:29510985, ECO:0000269|PubMed:31422817,
CC ECO:0000269|PubMed:31439631, ECO:0000269|PubMed:32354837}.
CC -!- INTERACTION:
CC Q9NRA8; P54253: ATXN1; NbExp=4; IntAct=EBI-301024, EBI-930964;
CC Q9NRA8; Q8IYR0: CFAP206; NbExp=3; IntAct=EBI-301024, EBI-749051;
CC Q9NRA8; P26196: DDX6; NbExp=6; IntAct=EBI-301024, EBI-351257;
CC Q9NRA8; Q9H4E7: DEF6; NbExp=3; IntAct=EBI-301024, EBI-745369;
CC Q9NRA8; Q86UW9: DTX2; NbExp=7; IntAct=EBI-301024, EBI-740376;
CC Q9NRA8; Q5JVL4: EFHC1; NbExp=9; IntAct=EBI-301024, EBI-743105;
CC Q9NRA8; P06730: EIF4E; NbExp=12; IntAct=EBI-301024, EBI-73440;
CC Q9NRA8; O60573: EIF4E2; NbExp=4; IntAct=EBI-301024, EBI-398610;
CC Q9NRA8; Q9NW38: FANCL; NbExp=3; IntAct=EBI-301024, EBI-2339898;
CC Q9NRA8; P52597: HNRNPF; NbExp=3; IntAct=EBI-301024, EBI-352986;
CC Q9NRA8; P08727: KRT19; NbExp=3; IntAct=EBI-301024, EBI-742756;
CC Q9NRA8; Q969R5: L3MBTL2; NbExp=3; IntAct=EBI-301024, EBI-739909;
CC Q9NRA8; O43482: OIP5; NbExp=3; IntAct=EBI-301024, EBI-536879;
CC Q9NRA8; P86480: PRR20D; NbExp=3; IntAct=EBI-301024, EBI-12754095;
CC Q9NRA8; Q7Z699: SPRED1; NbExp=3; IntAct=EBI-301024, EBI-5235340;
CC Q9NRA8; Q9BT92: TCHP; NbExp=3; IntAct=EBI-301024, EBI-740781;
CC Q9NRA8; Q6DKK2: TTC19; NbExp=3; IntAct=EBI-301024, EBI-948354;
CC Q9NRA8; P40222: TXLNA; NbExp=3; IntAct=EBI-301024, EBI-359793;
CC Q9NRA8; O75604: USP2; NbExp=3; IntAct=EBI-301024, EBI-743272;
CC Q9NRA8; PRO_0000037548 [Q9WMX2]; Xeno; NbExp=3; IntAct=EBI-301024, EBI-6863741;
CC -!- SUBCELLULAR LOCATION: Cytoplasm, P-body {ECO:0000269|PubMed:16157702,
CC ECO:0000269|PubMed:22966201, ECO:0000269|PubMed:23991149,
CC ECO:0000269|PubMed:24335285, ECO:0000269|PubMed:32354837}. Cytoplasm
CC {ECO:0000269|PubMed:10856257, ECO:0000269|PubMed:22090346,
CC ECO:0000269|PubMed:28216671}. Nucleus {ECO:0000269|PubMed:10856257,
CC ECO:0000269|PubMed:22090346, ECO:0000269|PubMed:28216671}. Nucleus, PML
CC body {ECO:0000269|PubMed:22090346}. Nucleus speckle
CC {ECO:0000269|PubMed:22090346}. Note=Predominantly cytoplasmic
CC (PubMed:10856257). Mainly localizes to processing bodies (P-bodies)
CC (PubMed:16157702). Shuttles between the nucleus and the cytoplasm in a
CC CRM1-dependent manner (PubMed:10856257). Localization to nuclear foci
CC and speckles requires active transcription (PubMed:22090346).
CC {ECO:0000269|PubMed:10856257, ECO:0000269|PubMed:16157702,
CC ECO:0000269|PubMed:22090346}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=3;
CC Name=1;
CC IsoId=Q9NRA8-1; Sequence=Displayed;
CC Name=2;
CC IsoId=Q9NRA8-2; Sequence=VSP_003783, VSP_003784, VSP_047042;
CC Name=3;
CC IsoId=Q9NRA8-3; Sequence=VSP_047042;
CC -!- TISSUE SPECIFICITY: Widely expressed. {ECO:0000269|PubMed:10856257}.
CC -!- DOMAIN: Intrinsically disordered protein with multiple low-complexity
CC regions that confer binding to multiple RNA translation, deadenylation
CC and decapping factors. {ECO:0000269|PubMed:27342281,
CC ECO:0000269|PubMed:28216671}.
CC -!- DOMAIN: The YXXXXLphi motif mediates interaction with eIF4E (EIF4E and
CC EIF4E2). {ECO:0000269|PubMed:10856257, ECO:0000269|PubMed:16157702,
CC ECO:0000269|PubMed:23991149, ECO:0000269|PubMed:24335285}.
CC -!- PTM: Phosphorylation by MAPK8/JNK1 and or MAPK9/JNK2 in response to
CC oxidative stress promotes P-body assembly (PubMed:22966201).
CC Phosphorylated during meiotic maturation (By similarity).
CC {ECO:0000250|UniProtKB:Q9EST3, ECO:0000269|PubMed:22966201}.
CC -!- SIMILARITY: Belongs to the 4E-T/EIF4E-T family. {ECO:0000305}.
CC -!- SEQUENCE CAUTION:
CC Sequence=BAB15092.1; Type=Erroneous initiation; Evidence={ECO:0000305};
CC Sequence=BAC11194.1; Type=Erroneous initiation; Evidence={ECO:0000305};
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; AF240775; AAF81693.1; -; mRNA.
DR EMBL; CR456386; CAG30272.1; -; mRNA.
DR EMBL; AK025254; BAB15092.1; ALT_INIT; mRNA.
DR EMBL; AK074768; BAC11194.1; ALT_INIT; mRNA.
DR EMBL; AK314636; BAG37198.1; -; mRNA.
DR EMBL; AL096701; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; CH471095; EAW59977.1; -; Genomic_DNA.
DR EMBL; BC032941; AAH32941.1; -; mRNA.
DR EMBL; BC033028; AAH33028.1; -; mRNA.
DR CCDS; CCDS13898.1; -. [Q9NRA8-1]
DR CCDS; CCDS54520.1; -. [Q9NRA8-2]
DR RefSeq; NP_001157973.1; NM_001164501.1. [Q9NRA8-1]
DR RefSeq; NP_001157974.1; NM_001164502.1. [Q9NRA8-2]
DR RefSeq; NP_062817.2; NM_019843.3. [Q9NRA8-1]
DR RefSeq; XP_005261743.1; XM_005261686.2. [Q9NRA8-3]
DR RefSeq; XP_005261744.1; XM_005261687.2. [Q9NRA8-3]
DR RefSeq; XP_005261745.1; XM_005261688.2. [Q9NRA8-3]
DR RefSeq; XP_011528582.1; XM_011530280.1. [Q9NRA8-1]
DR RefSeq; XP_011528583.1; XM_011530281.2. [Q9NRA8-3]
DR RefSeq; XP_016884353.1; XM_017028864.1. [Q9NRA8-1]
DR PDB; 5ANR; X-ray; 2.10 A; C=199-239.
DR PDB; 6F9W; X-ray; 2.62 A; B=954-985.
DR PDB; 6X2R; X-ray; 2.30 A; D=434-448.
DR PDBsum; 5ANR; -.
DR PDBsum; 6F9W; -.
DR PDBsum; 6X2R; -.
DR AlphaFoldDB; Q9NRA8; -.
DR SMR; Q9NRA8; -.
DR BioGRID; 121148; 296.
DR CORUM; Q9NRA8; -.
DR IntAct; Q9NRA8; 60.
DR MINT; Q9NRA8; -.
DR STRING; 9606.ENSP00000380659; -.
DR iPTMnet; Q9NRA8; -.
DR MetOSite; Q9NRA8; -.
DR PhosphoSitePlus; Q9NRA8; -.
DR BioMuta; EIF4ENIF1; -.
DR DMDM; 22095430; -.
DR EPD; Q9NRA8; -.
DR jPOST; Q9NRA8; -.
DR MassIVE; Q9NRA8; -.
DR MaxQB; Q9NRA8; -.
DR PaxDb; Q9NRA8; -.
DR PeptideAtlas; Q9NRA8; -.
DR PRIDE; Q9NRA8; -.
DR ProteomicsDB; 3074; -.
DR ProteomicsDB; 82323; -. [Q9NRA8-1]
DR ProteomicsDB; 82324; -. [Q9NRA8-2]
DR Antibodypedia; 279; 310 antibodies from 30 providers.
DR DNASU; 56478; -.
DR Ensembl; ENST00000330125.10; ENSP00000328103.5; ENSG00000184708.18. [Q9NRA8-1]
DR Ensembl; ENST00000344710.9; ENSP00000342927.5; ENSG00000184708.18. [Q9NRA8-2]
DR Ensembl; ENST00000397525.5; ENSP00000380659.1; ENSG00000184708.18. [Q9NRA8-1]
DR GeneID; 56478; -.
DR KEGG; hsa:56478; -.
DR MANE-Select; ENST00000330125.10; ENSP00000328103.5; NM_019843.4; NP_062817.2.
DR UCSC; uc003akz.3; human. [Q9NRA8-1]
DR CTD; 56478; -.
DR DisGeNET; 56478; -.
DR GeneCards; EIF4ENIF1; -.
DR HGNC; HGNC:16687; EIF4ENIF1.
DR HPA; ENSG00000184708; Low tissue specificity.
DR MIM; 607445; gene.
DR neXtProt; NX_Q9NRA8; -.
DR OpenTargets; ENSG00000184708; -.
DR Orphanet; 619; NON RARE IN EUROPE: Primary ovarian failure.
DR PharmGKB; PA38410; -.
DR VEuPathDB; HostDB:ENSG00000184708; -.
DR eggNOG; ENOG502QRQE; Eukaryota.
DR GeneTree; ENSGT00390000012071; -.
DR InParanoid; Q9NRA8; -.
DR OMA; MLSQGVH; -.
DR OrthoDB; 198628at2759; -.
DR PhylomeDB; Q9NRA8; -.
DR TreeFam; TF101531; -.
DR PathwayCommons; Q9NRA8; -.
DR SignaLink; Q9NRA8; -.
DR SIGNOR; Q9NRA8; -.
DR BioGRID-ORCS; 56478; 50 hits in 1087 CRISPR screens.
DR ChiTaRS; EIF4ENIF1; human.
DR GeneWiki; EIF4ENIF1; -.
DR GenomeRNAi; 56478; -.
DR Pharos; Q9NRA8; Tbio.
DR PRO; PR:Q9NRA8; -.
DR Proteomes; UP000005640; Chromosome 22.
DR RNAct; Q9NRA8; protein.
DR Bgee; ENSG00000184708; Expressed in secondary oocyte and 194 other tissues.
DR ExpressionAtlas; Q9NRA8; baseline and differential.
DR Genevisible; Q9NRA8; HS.
DR GO; GO:0005737; C:cytoplasm; IDA:UniProtKB.
DR GO; GO:0005829; C:cytosol; IEA:Ensembl.
DR GO; GO:0043231; C:intracellular membrane-bounded organelle; IDA:HPA.
DR GO; GO:0016020; C:membrane; HDA:UniProtKB.
DR GO; GO:0016607; C:nuclear speck; IEA:UniProtKB-SubCell.
DR GO; GO:0005634; C:nucleus; IDA:UniProtKB.
DR GO; GO:0000932; C:P-body; IDA:UniProtKB.
DR GO; GO:0016605; C:PML body; IEA:UniProtKB-SubCell.
DR GO; GO:0019900; F:kinase binding; IPI:UniProtKB.
DR GO; GO:0003729; F:mRNA binding; IBA:GO_Central.
DR GO; GO:0005049; F:nuclear export signal receptor activity; IDA:GO_Central.
DR GO; GO:0003723; F:RNA binding; HDA:UniProtKB.
DR GO; GO:0035278; P:miRNA-mediated gene silencing by inhibition of translation; IDA:UniProtKB.
DR GO; GO:0048255; P:mRNA stabilization; IDA:UniProtKB.
DR GO; GO:0106289; P:negative regulation of deadenylation-dependent decapping of nuclear-transcribed mRNA; IDA:UniProtKB.
DR GO; GO:0045665; P:negative regulation of neuron differentiation; IEA:Ensembl.
DR GO; GO:0017148; P:negative regulation of translation; IDA:UniProtKB.
DR GO; GO:0030182; P:neuron differentiation; IEA:Ensembl.
DR GO; GO:0033962; P:P-body assembly; IDA:UniProtKB.
DR GO; GO:0060213; P:positive regulation of nuclear-transcribed mRNA poly(A) tail shortening; IDA:UniProtKB.
DR GO; GO:0006606; P:protein import into nucleus; IDA:UniProtKB.
DR GO; GO:0019827; P:stem cell population maintenance; IEA:Ensembl.
DR GO; GO:0006412; P:translation; IEA:Ensembl.
DR InterPro; IPR018862; eIF4E-T.
DR PANTHER; PTHR12269; PTHR12269; 1.
DR Pfam; PF10477; EIF4E-T; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Acetylation; Alternative splicing; Cytoplasm;
KW Isopeptide bond; Nucleus; Phosphoprotein; Protein transport;
KW Reference proteome; RNA-mediated gene silencing; Translation regulation;
KW Transport; Ubl conjugation.
FT CHAIN 1..985
FT /note="Eukaryotic translation initiation factor 4E
FT transporter"
FT /id="PRO_0000064381"
FT REGION 1..24
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 131..161
FT /note="Interaction with CSDE1"
FT /evidence="ECO:0000269|PubMed:27342281"
FT REGION 208..230
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 219..240
FT /note="Interaction with DDX6"
FT /evidence="ECO:0000269|PubMed:27342281"
FT REGION 448..490
FT /note="Interaction with LSM14A"
FT /evidence="ECO:0000269|PubMed:26027925"
FT REGION 664..693
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 695..713
FT /note="Interaction with PATL1"
FT /evidence="ECO:0000269|PubMed:26027925"
FT REGION 707..803
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 922..953
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 940..985
FT /note="Interaction with LSM14A"
FT /evidence="ECO:0000269|PubMed:26027925"
FT MOTIF 30..36
FT /note="YXXXXLphi motif"
FT /evidence="ECO:0000269|PubMed:10856257,
FT ECO:0000269|PubMed:24335285"
FT MOTIF 195..211
FT /note="Nuclear localization signal"
FT /evidence="ECO:0000305|PubMed:10856257"
FT MOTIF 438..447
FT /note="Nuclear export signal"
FT /evidence="ECO:0000305|PubMed:10856257"
FT MOTIF 613..638
FT /note="Nuclear export signal"
FT /evidence="ECO:0000305|PubMed:10856257"
FT COMPBIAS 1..15
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 665..693
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 707..734
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 735..778
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 5
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:19690332,
FT ECO:0007744|PubMed:20068231, ECO:0007744|PubMed:23186163"
FT MOD_RES 74
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:23186163"
FT MOD_RES 78
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:23186163"
FT MOD_RES 115
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:23186163"
FT MOD_RES 120
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:18669648"
FT MOD_RES 136
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:18669648"
FT MOD_RES 138
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:18669648"
FT MOD_RES 301
FT /note="Phosphoserine"
FT /evidence="ECO:0000269|PubMed:22966201,
FT ECO:0007744|PubMed:20068231"
FT MOD_RES 345
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:18669648"
FT MOD_RES 353
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:24275569"
FT MOD_RES 374
FT /note="Phosphoserine"
FT /evidence="ECO:0000269|PubMed:22966201"
FT MOD_RES 417
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:23186163"
FT MOD_RES 486
FT /note="N6-acetyllysine"
FT /evidence="ECO:0007744|PubMed:19608861"
FT MOD_RES 513
FT /note="Phosphoserine"
FT /evidence="ECO:0000269|PubMed:22966201,
FT ECO:0007744|PubMed:20068231, ECO:0007744|PubMed:23186163"
FT MOD_RES 564
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:18669648,
FT ECO:0007744|PubMed:19690332, ECO:0007744|PubMed:20068231,
FT ECO:0007744|PubMed:23186163"
FT MOD_RES 587
FT /note="Phosphoserine"
FT /evidence="ECO:0000269|PubMed:22966201,
FT ECO:0007744|PubMed:19690332, ECO:0007744|PubMed:23186163"
FT MOD_RES 693
FT /note="Phosphoserine"
FT /evidence="ECO:0000269|PubMed:22966201,
FT ECO:0007744|PubMed:19690332"
FT MOD_RES 752
FT /note="Phosphoserine"
FT /evidence="ECO:0000269|PubMed:22966201"
FT MOD_RES 920
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:18088087"
FT MOD_RES 951
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:18669648,
FT ECO:0007744|PubMed:20068231, ECO:0007744|PubMed:21406692,
FT ECO:0007744|PubMed:23186163, ECO:0007744|PubMed:24275569"
FT CROSSLNK 410
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2)"
FT /evidence="ECO:0007744|PubMed:28112733"
FT VAR_SEQ 100..262
FT /note="Missing (in isoform 2)"
FT /evidence="ECO:0000303|PubMed:15489334"
FT /id="VSP_003783"
FT VAR_SEQ 493..504
FT /note="Missing (in isoform 2)"
FT /evidence="ECO:0000303|PubMed:15489334"
FT /id="VSP_003784"
FT VAR_SEQ 616
FT /note="Q -> QQ (in isoform 2 and isoform 3)"
FT /evidence="ECO:0000303|PubMed:14702039,
FT ECO:0000303|PubMed:15489334"
FT /id="VSP_047042"
FT MUTAGEN 30..36
FT /note="YTKEELL->ATKEEAA: Abolished interaction with
FT EIF4E2."
FT /evidence="ECO:0000269|PubMed:23991149,
FT ECO:0000269|PubMed:28487484"
FT MUTAGEN 30
FT /note="Y->A: Abolishes interaction with EIF4E and EIF4E2.
FT Impaired ability to repress mRNA translation."
FT /evidence="ECO:0000269|PubMed:10856257,
FT ECO:0000269|PubMed:16157702, ECO:0000269|PubMed:24335285,
FT ECO:0000269|PubMed:28487484"
FT MUTAGEN 35..36
FT /note="LL->AA: Abolished interaction with EIF4E2."
FT /evidence="ECO:0000269|PubMed:23991149"
FT MUTAGEN 54..61
FT /note="KYDSDGVW->ADSDAA: Strongly reduced interaction with
FT EIF4E and EIF4E2."
FT /evidence="ECO:0000269|PubMed:23991149"
FT MUTAGEN 195..196
FT /note="RR->NS: Abolishes the nuclear localization."
FT /evidence="ECO:0000269|PubMed:10856257"
FT MUTAGEN 301
FT /note="S->A: In S6A mutant; abolished phosphorylation by
FT MAPK8/JNK1; impaired P-body assembly in response to
FT oxidative stress when associated with A-374, A-513, A-587,
FT A-693 and A-752."
FT /evidence="ECO:0000269|PubMed:22966201"
FT MUTAGEN 374
FT /note="S->A: In S6A mutant; abolished phosphorylation by
FT MAPK8/JNK1; impaired P-body assembly in response to
FT oxidative stress when associated with A-301, A-513, A-587,
FT A-693 and A-752."
FT /evidence="ECO:0000269|PubMed:22966201"
FT MUTAGEN 513
FT /note="S->A: In S6A mutant; abolished phosphorylation by
FT MAPK8/JNK1; impaired P-body assembly in response to
FT oxidative stress when associated with A-301, A-374, A-587,
FT A-693 and A-752."
FT /evidence="ECO:0000269|PubMed:22966201"
FT MUTAGEN 587
FT /note="S->A: In S6A mutant; abolished phosphorylation by
FT MAPK8/JNK1; impaired P-body assembly in response to
FT oxidative stress when associated with A-301, A-374, A-513,
FT A-693 and A-752."
FT /evidence="ECO:0000269|PubMed:22966201"
FT MUTAGEN 693
FT /note="S->A: In S6A mutant; abolished phosphorylation by
FT MAPK8/JNK1; impaired P-body assembly in response to
FT oxidative stress when associated with A-301, A-374, A-513,
FT A-587 and A-752."
FT /evidence="ECO:0000269|PubMed:22966201"
FT MUTAGEN 752
FT /note="S->A: In S6A mutant; abolished phosphorylation by
FT MAPK8/JNK1; impaired P-body assembly in response to
FT oxidative stress when associated with A-301, A-374, A-513,
FT A-587 and A-693."
FT /evidence="ECO:0000269|PubMed:22966201"
FT MUTAGEN 955..958
FT /note="LAKW->AAKA: Abolished interaction with LSM14A."
FT /evidence="ECO:0000269|PubMed:29510985"
FT MUTAGEN 958
FT /note="W->A: Abolished interaction with LSM14A."
FT /evidence="ECO:0000269|PubMed:29510985"
FT MUTAGEN 959
FT /note="F->A: Abolished interaction with LSM14A."
FT /evidence="ECO:0000269|PubMed:29510985"
FT MUTAGEN 961
FT /note="S->A: Does not affect interaction with LSM14A."
FT /evidence="ECO:0000269|PubMed:29510985"
FT MUTAGEN 970
FT /note="S->A: Does not affect interaction with LSM14A."
FT /evidence="ECO:0000269|PubMed:29510985"
FT MUTAGEN 978..981
FT /note="VDEL->ADEA: Abolished interaction with LSM14A."
FT /evidence="ECO:0000269|PubMed:29510985"
FT MUTAGEN 978
FT /note="V->A: Abolished interaction with LSM14A."
FT /evidence="ECO:0000269|PubMed:29510985"
FT MUTAGEN 982
FT /note="E->K: Abolished interaction with LSM14A."
FT /evidence="ECO:0000269|PubMed:29510985"
FT CONFLICT 114
FT /note="L -> F (in Ref. 1; AAF81693)"
FT /evidence="ECO:0000305"
FT CONFLICT 825
FT /note="Q -> R (in Ref. 6; AAH33028)"
FT /evidence="ECO:0000305"
FT HELIX 220..223
FT /evidence="ECO:0007829|PDB:5ANR"
FT HELIX 435..443
FT /evidence="ECO:0007829|PDB:6X2R"
FT HELIX 955..957
FT /evidence="ECO:0007829|PDB:6F9W"
FT HELIX 961..965
FT /evidence="ECO:0007829|PDB:6F9W"
FT STRAND 975..977
FT /evidence="ECO:0007829|PDB:6F9W"
FT HELIX 978..984
FT /evidence="ECO:0007829|PDB:6F9W"
SQ SEQUENCE 985 AA; 108201 MW; 4C898E0488903C04 CRC64;
MDRRSMGETE SGDAFLDLKK PPASKCPHRY TKEELLDIKE LPHSKQRPSC LSEKYDSDGV
WDPEKWHASL YPASGRSSPV ESLKKELDTD RPSLVRRIVD PRERVKEDDL DVVLSPQRRS
FGGGCHVTAA VSSRRSGSPL EKDSDGLRLL GGRRIGSGRI ISARTFEKDH RLSDKDLRDL
RDRDRERDFK DKRFRREFGD SKRVFGERRR NDSYTEEEPE WFSAGPTSQS ETIELTGFDD
KILEEDHKGR KRTRRRTASV KEGIVECNGG VAEEDEVEVI LAQEPAADQE VPRDAVLPEQ
SPGDFDFNEF FNLDKVPCLA SMIEDVLGEG SVSASRFSRW FSNPSRSGSR SSSLGSTPHE
ELERLAGLEQ AILSPGQNSG NYFAPIPLED HAENKVDILE MLQKAKVDLK PLLSSLSANK
EKLKESSHSG VVLSVEEVEA GLKGLKVDQQ VKNSTPFMAE HLEETLSAVT NNRQLKKDGD
MTAFNKLVST MKASGTLPSQ PKVSRNLESH LMSPAEIPGQ PVPKNILQEL LGQPVQRPAS
SNLLSGLMGS LEPTTSLLGQ RAPSPPLSQV FQTRAASADY LRPRIPSPIG FTPGPQQLLG
DPFQGMRKPM SPITAQMSQL ELQQAALEGL ALPHDLAVQA ANFYQPGFGK PQVDRTRDGF
RNRQQRVTKS PAPVHRGNSS SPAPAASITS MLSPSFTPTS VIRKMYESKE KSKEEPASGK
AALGDSKEDT QKASEENLLS SSSVPSADRD SSPTTNSKLS ALQRSSCSTP LSQANRYTKE
QDYRPKATGR KTPTLASPVP TTPFLRPVHQ VPLVPHVPMV RPAHQLHPGL VQRMLAQGVH
PQHLPSLLQT GVLPPGMDLS HLQGISGPIL GQPFYPLPAA SHPLLNPRPG TPLHLAMVQQ
QLQRSVLHPP GSGSHAAAVS VQTTPQNVPS RSGLPHMHSQ LEHRPSQRSS SPVGLAKWFG
SDVLQQPLPS MPAKVISVDE LEYRQ
