4ET_MOUSE
ID 4ET_MOUSE Reviewed; 983 AA.
AC Q9EST3; Q8CFW0; Q9CSS3;
DT 02-AUG-2002, integrated into UniProtKB/Swiss-Prot.
DT 27-JUL-2011, sequence version 2.
DT 03-AUG-2022, entry version 141.
DE RecName: Full=Eukaryotic translation initiation factor 4E transporter {ECO:0000303|PubMed:25456498};
DE Short=4E-T {ECO:0000303|PubMed:25456498};
DE Short=eIF4E transporter {ECO:0000303|PubMed:25456498};
DE AltName: Full=CD40 ligand-activated specific transcript 4 {ECO:0000303|Ref.1};
DE AltName: Full=Eukaryotic translation initiation factor 4E nuclear import factor 1;
GN Name=Eif4enif1 {ECO:0000312|MGI:MGI:1921453};
GN Synonyms=Clast4 {ECO:0000303|PubMed:16343815, ECO:0000303|Ref.1};
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] (ISOFORM 1).
RA O-Wang J.;
RT "Cloning and characterization of a novel CD40-activated gene.";
RL Submitted (AUG-1999) to the EMBL/GenBank/DDBJ databases.
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=C57BL/6J;
RX PubMed=19468303; DOI=10.1371/journal.pbio.1000112;
RA Church D.M., Goodstadt L., Hillier L.W., Zody M.C., Goldstein S., She X.,
RA Bult C.J., Agarwala R., Cherry J.L., DiCuccio M., Hlavina W., Kapustin Y.,
RA Meric P., Maglott D., Birtle Z., Marques A.C., Graves T., Zhou S.,
RA Teague B., Potamousis K., Churas C., Place M., Herschleb J., Runnheim R.,
RA Forrest D., Amos-Landgraf J., Schwartz D.C., Cheng Z., Lindblad-Toh K.,
RA Eichler E.E., Ponting C.P.;
RT "Lineage-specific biology revealed by a finished genome assembly of the
RT mouse.";
RL PLoS Biol. 7:E1000112-E1000112(2009).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RA Mural R.J., Adams M.D., Myers E.W., Smith H.O., Venter J.C.;
RL Submitted (JUL-2005) to the EMBL/GenBank/DDBJ databases.
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
RC TISSUE=Eye;
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 [5]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 428-983 (ISOFORM 2).
RC STRAIN=C57BL/6J; TISSUE=Embryo;
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 [6]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-586, AND IDENTIFICATION BY
RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Embryonic brain;
RX PubMed=15345747; DOI=10.1074/mcp.m400085-mcp200;
RA Ballif B.A., Villen J., Beausoleil S.A., Schwartz D., Gygi S.P.;
RT "Phosphoproteomic analysis of the developing mouse brain.";
RL Mol. Cell. Proteomics 3:1093-1101(2004).
RN [7]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-949, AND IDENTIFICATION BY
RP 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 [8]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-563 AND SER-586, AND
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Brain, Kidney, Lung, 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, INTERACTION WITH EIF4E, TISSUE SPECIFICITY,
RP ALTERNATIVE SPLICING, AND MUTAGENESIS OF 29-TYR--LEU-34.
RX PubMed=16343815; DOI=10.1016/j.gene.2005.09.026;
RA Villaescusa J.C., Allard P., Carminati E., Kontogiannea M., Talarico D.,
RA Blasi F., Farookhi R., Verrotti A.C.;
RT "Clast4, the murine homologue of human eIF4E-transporter, is highly
RT expressed in developing oocytes and post-translationally modified at
RT meiotic maturation.";
RL Gene 367:101-109(2006).
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).
CC -!- FUNCTION: EIF4E-binding protein that regulates translation and
CC stability of mRNAs in processing bodies (P-bodies) (PubMed:25456498).
CC Plays a key role in P-bodies to coordinate the storage of
CC translationally inactive mRNAs in the cytoplasm and prevent their
CC degradation (By similarity). Acts as a binding platform for multiple
CC RNA-binding proteins: promotes deadenylation of mRNAs via its
CC interaction with the CCR4-NOT complex, and blocks decapping via
CC interaction with eIF4E (EIF4E and EIF4E2), thereby protecting
CC deadenylated and repressed mRNAs from degradation (By similarity).
CC Component of a multiprotein complex that sequesters and represses
CC translation of proneurogenic factors during neurogenesis
CC (PubMed:25456498). Promotes miRNA-mediated translational repression (By
CC similarity). Involved in mRNA translational repression mediated by the
CC miRNA effector TNRC6B by protecting TNRC6B-targeted mRNAs from
CC decapping and subsequent decay (By similarity). Required for the
CC formation of P-bodies (By similarity). Also acts as a nucleoplasmic
CC shuttling protein, which mediates the nuclear import of EIF4E and DDX6
CC by a piggy-back mechanism (By similarity).
CC {ECO:0000250|UniProtKB:Q9NRA8, ECO:0000269|PubMed:25456498}.
CC -!- SUBUNIT: Interacts (via YXXXXLphi motif) with EIF4E (PubMed:16343815).
CC Interacts (via YXXXXLphi motif) with EIF4E2 (By similarity). Interacts
CC with DDX6. Interacts with CSDE1/UNR (By similarity). Interacts with
CC CNOT1; promoting association with the CCR4-NOT complex (By similarity).
CC Interacts with LSM14A; promoting EIF4ENIF1 localization to P-bodies (By
CC similarity). Interacts with PATL1 (By similarity). Interacts with
CC importin beta only in the presence of importin alpha, suggesting a
CC direct interaction with importin alpha (By similarity). Interacts with
CC APOBEC3G in an RNA-dependent manner (By similarity).
CC {ECO:0000250|UniProtKB:Q9NRA8, ECO:0000269|PubMed:16343815}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000269|PubMed:16343815}. Nucleus
CC {ECO:0000250|UniProtKB:Q9NRA8}. Nucleus, PML body
CC {ECO:0000250|UniProtKB:Q9NRA8}. Nucleus speckle
CC {ECO:0000250|UniProtKB:Q9NRA8}. Note=Predominantly cytoplasmic (By
CC similarity). Mainly localizes to processing bodies (P-bodies) (By
CC similarity). Shuttles between the nucleus and the cytoplasm in a CRM1-
CC dependent manner. Localization to nuclear foci and speckles requires
CC active transcription (By similarity). {ECO:0000250|UniProtKB:Q9NRA8}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=2;
CC Name=1; Synonyms=Clast4-L {ECO:0000303|PubMed:16343815};
CC IsoId=Q9EST3-1; Sequence=Displayed;
CC Name=2; Synonyms=Clast4-S {ECO:0000303|PubMed:16343815};
CC IsoId=Q9EST3-2; Sequence=VSP_003785;
CC -!- TISSUE SPECIFICITY: Highly expressed in developing oocytes.
CC {ECO:0000269|PubMed:16343815}.
CC -!- DOMAIN: Intrinsically disordered protein with multiple low-complexity
CC regions that confer binding to multiple RNA translation, deadenylation
CC and decapping factors. {ECO:0000250|UniProtKB:Q9NRA8}.
CC -!- DOMAIN: The YXXXXLphi motif mediates interaction with eIF4E (EIF4E and
CC EIF4E2). {ECO:0000250|UniProtKB:Q9NRA8}.
CC -!- PTM: Phosphorylation by MAPK8/JNK1 and or MAPK9/JNK2 in response to
CC oxidative stress promotes P-body assembly (By similarity).
CC Phosphorylated during meiotic maturation (PubMed:16343815).
CC {ECO:0000250|UniProtKB:Q9NRA8, ECO:0000269|PubMed:16343815}.
CC -!- SIMILARITY: Belongs to the 4E-T/EIF4E-T family. {ECO:0000305}.
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DR EMBL; AB031388; BAB11963.1; -; mRNA.
DR EMBL; AL671968; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; CH466574; EDL40398.1; -; Genomic_DNA.
DR EMBL; BC033410; AAH33410.1; -; mRNA.
DR EMBL; AK012082; BAB28016.1; -; mRNA.
DR CCDS; CCDS24354.1; -. [Q9EST3-1]
DR CCDS; CCDS48739.1; -. [Q9EST3-2]
DR RefSeq; NP_001160019.1; NM_001166547.1. [Q9EST3-1]
DR RefSeq; NP_001160020.1; NM_001166548.1. [Q9EST3-2]
DR RefSeq; NP_001160021.1; NM_001166549.1. [Q9EST3-2]
DR RefSeq; NP_076232.2; NM_023743.2. [Q9EST3-1]
DR RefSeq; XP_006514904.1; XM_006514841.2. [Q9EST3-1]
DR RefSeq; XP_006514905.1; XM_006514842.3. [Q9EST3-1]
DR RefSeq; XP_006514906.1; XM_006514843.3. [Q9EST3-1]
DR RefSeq; XP_006514907.1; XM_006514844.2. [Q9EST3-2]
DR RefSeq; XP_017170295.1; XM_017314806.1. [Q9EST3-2]
DR AlphaFoldDB; Q9EST3; -.
DR SMR; Q9EST3; -.
DR BioGRID; 216574; 10.
DR STRING; 10090.ENSMUSP00000105676; -.
DR iPTMnet; Q9EST3; -.
DR PhosphoSitePlus; Q9EST3; -.
DR EPD; Q9EST3; -.
DR jPOST; Q9EST3; -.
DR MaxQB; Q9EST3; -.
DR PaxDb; Q9EST3; -.
DR PeptideAtlas; Q9EST3; -.
DR PRIDE; Q9EST3; -.
DR ProteomicsDB; 296447; -. [Q9EST3-1]
DR ProteomicsDB; 296448; -. [Q9EST3-2]
DR Antibodypedia; 279; 310 antibodies from 30 providers.
DR DNASU; 74203; -.
DR Ensembl; ENSMUST00000020734; ENSMUSP00000020734; ENSMUSG00000020454. [Q9EST3-2]
DR Ensembl; ENSMUST00000110048; ENSMUSP00000105675; ENSMUSG00000020454. [Q9EST3-2]
DR Ensembl; ENSMUST00000110049; ENSMUSP00000105676; ENSMUSG00000020454. [Q9EST3-1]
DR Ensembl; ENSMUST00000179770; ENSMUSP00000136768; ENSMUSG00000020454. [Q9EST3-1]
DR GeneID; 74203; -.
DR KEGG; mmu:74203; -.
DR UCSC; uc007hsc.2; mouse. [Q9EST3-2]
DR UCSC; uc007hse.2; mouse. [Q9EST3-1]
DR CTD; 56478; -.
DR MGI; MGI:1921453; Eif4enif1.
DR VEuPathDB; HostDB:ENSMUSG00000020454; -.
DR eggNOG; ENOG502QRQE; Eukaryota.
DR GeneTree; ENSGT00390000012071; -.
DR HOGENOM; CLU_014394_0_0_1; -.
DR InParanoid; Q9EST3; -.
DR OMA; MLSQGVH; -.
DR OrthoDB; 198628at2759; -.
DR PhylomeDB; Q9EST3; -.
DR TreeFam; TF101531; -.
DR BioGRID-ORCS; 74203; 12 hits in 71 CRISPR screens.
DR ChiTaRS; Eif4enif1; mouse.
DR PRO; PR:Q9EST3; -.
DR Proteomes; UP000000589; Chromosome 11.
DR RNAct; Q9EST3; protein.
DR Bgee; ENSMUSG00000020454; Expressed in animal zygote and 263 other tissues.
DR ExpressionAtlas; Q9EST3; baseline and differential.
DR Genevisible; Q9EST3; MM.
DR GO; GO:0005737; C:cytoplasm; IDA:MGI.
DR GO; GO:0005829; C:cytosol; IDA:MGI.
DR GO; GO:0043231; C:intracellular membrane-bounded organelle; ISO:MGI.
DR GO; GO:0016607; C:nuclear speck; IEA:UniProtKB-SubCell.
DR GO; GO:0005634; C:nucleus; IDA:MGI.
DR GO; GO:0000932; C:P-body; IDA:MGI.
DR GO; GO:0016605; C:PML body; IEA:UniProtKB-SubCell.
DR GO; GO:0019900; F:kinase binding; ISO:MGI.
DR GO; GO:0003729; F:mRNA binding; IDA:MGI.
DR GO; GO:0005049; F:nuclear export signal receptor activity; ISO:MGI.
DR GO; GO:0035278; P:miRNA-mediated gene silencing by inhibition of translation; ISS:UniProtKB.
DR GO; GO:0048255; P:mRNA stabilization; ISS:UniProtKB.
DR GO; GO:0106289; P:negative regulation of deadenylation-dependent decapping of nuclear-transcribed mRNA; ISS:UniProtKB.
DR GO; GO:0045665; P:negative regulation of neuron differentiation; IGI:MGI.
DR GO; GO:0017148; P:negative regulation of translation; IMP:MGI.
DR GO; GO:0030182; P:neuron differentiation; IGI:MGI.
DR GO; GO:0033962; P:P-body assembly; ISS:UniProtKB.
DR GO; GO:0060213; P:positive regulation of nuclear-transcribed mRNA poly(A) tail shortening; ISS:UniProtKB.
DR GO; GO:0006606; P:protein import into nucleus; ISS:UniProtKB.
DR GO; GO:0019827; P:stem cell population maintenance; IGI:MGI.
DR GO; GO:0006412; P:translation; IMP:MGI.
DR InterPro; IPR018862; eIF4E-T.
DR PANTHER; PTHR12269; PTHR12269; 1.
DR Pfam; PF10477; EIF4E-T; 1.
PE 1: Evidence at protein level;
KW Acetylation; Alternative splicing; Cytoplasm; Isopeptide bond; Nucleus;
KW Phosphoprotein; Protein transport; Reference proteome;
KW RNA-mediated gene silencing; Translation regulation; Transport;
KW Ubl conjugation.
FT CHAIN 1..983
FT /note="Eukaryotic translation initiation factor 4E
FT transporter"
FT /id="PRO_0000064382"
FT REGION 1..22
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 40..99
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 130..160
FT /note="Interaction with CSDE1"
FT /evidence="ECO:0000250|UniProtKB:Q9NRA8"
FT REGION 206..229
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 218..239
FT /note="Interaction with DDX6"
FT /evidence="ECO:0000250|UniProtKB:Q9NRA8"
FT REGION 341..360
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 447..489
FT /note="Interaction with LSM14A"
FT /evidence="ECO:0000250|UniProtKB:Q9NRA8"
FT REGION 585..616
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 642..693
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 694..712
FT /note="Interaction with PATL1"
FT /evidence="ECO:0000250|UniProtKB:Q9NRA8"
FT REGION 708..800
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 906..951
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 938..983
FT /note="Interaction with LSM14A"
FT /evidence="ECO:0000250|UniProtKB:Q9NRA8"
FT MOTIF 29..35
FT /note="YXXXXLphi motif"
FT /evidence="ECO:0000269|PubMed:16343815"
FT MOTIF 194..210
FT /note="Nuclear localization signal"
FT /evidence="ECO:0000250|UniProtKB:Q9NRA8"
FT MOTIF 437..446
FT /note="Nuclear export signal"
FT /evidence="ECO:0000250|UniProtKB:Q9NRA8"
FT MOTIF 612..637
FT /note="Nuclear export signal"
FT /evidence="ECO:0000250|UniProtKB:Q9NRA8"
FT COMPBIAS 80..99
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 341..357
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 664..693
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 734..776
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 906..932
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 4
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q9NRA8"
FT MOD_RES 73
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q9NRA8"
FT MOD_RES 77
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q9NRA8"
FT MOD_RES 114
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q9NRA8"
FT MOD_RES 119
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q9NRA8"
FT MOD_RES 135
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q9NRA8"
FT MOD_RES 137
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q9NRA8"
FT MOD_RES 300
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q9NRA8"
FT MOD_RES 344
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q9NRA8"
FT MOD_RES 352
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q9NRA8"
FT MOD_RES 373
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q9NRA8"
FT MOD_RES 416
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q9NRA8"
FT MOD_RES 485
FT /note="N6-acetyllysine"
FT /evidence="ECO:0000250|UniProtKB:Q9NRA8"
FT MOD_RES 563
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:21183079"
FT MOD_RES 586
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q9NRA8"
FT MOD_RES 692
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q9NRA8"
FT MOD_RES 751
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q9NRA8"
FT MOD_RES 919
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q9NRA8"
FT MOD_RES 949
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:19144319"
FT CROSSLNK 409
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2)"
FT /evidence="ECO:0000250|UniProtKB:Q9NRA8"
FT VAR_SEQ 504..527
FT /note="Missing (in isoform 2)"
FT /evidence="ECO:0000303|PubMed:16141072"
FT /id="VSP_003785"
FT MUTAGEN 29..34
FT /note="YTKEEL->ATKEEA: Abolished interaction with EIF4E."
FT /evidence="ECO:0000269|PubMed:16343815"
FT CONFLICT 345
FT /note="R -> Q (in Ref. 1; BAB11963)"
FT /evidence="ECO:0000305"
FT CONFLICT 773
FT /note="S -> N (in Ref. 1; BAB11963)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 983 AA; 107986 MW; C010A10376699DA8 CRC64;
MEKSVAETEN GDAFLELKKL PTSKSPHRYT KEELLDIKER PYSKQRPSCL SEKYDSDGVW
DPEKWHASLY PASGRSSPVE SLKKESESDR PSLVRRIADP RERVKEDDLD VVLSPQRRSF
GGGCHVTAAV SSRRSGSPLE KDSDGLRLLG GRRIGSGRII SARAFEKDHR LSDKDLRDLR
DRDRERDYKD KRFRREFGDS KRVFGERRRN DSYTEEEPEW FSAGPTSQSE TIELTGFDDK
ILEEDHKGRK RTRRRTASVK EGIVECNGGV AEEDEVEVIL AQEPSADQEV PRDVILPEQS
PGEFDFNEFF NLDKVPCLAS MIEDVLGEGS VSASRFSRWF SNPSRSGSRS SSLGSTPHEE
LERLAGLEQA VLSPGQNSGN YFAPIPSEDH AENKVDILEM LQKAKVDLKP LLSSLSANKE
KLKESSHSGV VLSVEEVEAG LKGLKVDQQM KNSTPFMAEH LEETLSAASS NRQLKKDGDM
TAFNKLVNTM KASGTLPTQP KVSRNVESHL LAPAEIPGQP VSKNILQELL GQPVQRPASS
NLLSGLMGSL EATASLLSQR APSPPMSQVF RTQAASADYL HPRIPSPIGF PSGPQQLLGD
PFQGMRKPMS PVSAQMSQLE LQQAALEGLA LPHDLAVQTA PFYQPGFSKP QVDRTRDGLR
NRQQRMSKSP APMHGGNSSS PAPAASITSM LSPSFTPTSV IRKMYESREK TKEEMAPGMV
VPGDGKEDTQ KTSEENLLSS NPIPNTDQDS STTNPKLSTL QRSSCSTPLS QTSRYTKEQD
YRPKTAGRKT PTLASPVPGT PFLRPTHQVP LVPHVPIVRP AHQLHPGLVQ RLIAQGVHPQ
HLPSLLQAGV LPPGIDMAPL QGLSGPLLGQ PLYPLVSAAS HPLLNPRPGT PLHLAVMQQQ
LQRSVLHPPG SSSQAAAISV QTPQNVPSRS GMPHMHSQLE HRTSQRSSSP VGLAKWFGSD
VLQQPLPSMP TKVISVDELE YRQ
