EF1A1_MOUSE
ID EF1A1_MOUSE Reviewed; 462 AA.
AC P10126; Q61511; Q6ZWN2; Q8BMB8; Q8BVS8; Q99KU5;
DT 01-JUL-1989, integrated into UniProtKB/Swiss-Prot.
DT 25-OCT-2004, sequence version 3.
DT 03-AUG-2022, entry version 225.
DE RecName: Full=Elongation factor 1-alpha 1;
DE Short=EF-1-alpha-1;
DE AltName: Full=Elongation factor Tu;
DE Short=EF-Tu;
DE AltName: Full=Eukaryotic elongation factor 1 A-1;
DE Short=eEF1A-1;
GN Name=Eef1a1; Synonyms=Eef1a;
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=3215517; DOI=10.1016/0378-1119(88)90195-3;
RA Reddy N.S., Roth W.W., Bragg P.W., Wahba A.J.;
RT "Isolation and mapping of a gene for protein synthesis initiation factor 4A
RT and its expression during differentiation of murine erythroleukemia
RT cells.";
RL Gene 70:231-243(1988).
RN [2]
RP NUCLEOTIDE SEQUENCE [MRNA].
RX PubMed=2911475; DOI=10.1093/nar/17.1.442;
RA Lu X., Werner D.;
RT "The complete cDNA sequence of mouse elongation factor 1 alpha (EF 1 alpha)
RT mRNA.";
RL Nucleic Acids Res. 17:442-442(1989).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=C57BL/6J; TISSUE=Head, Testis, and Thymus;
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 [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=Czech II; TISSUE=Mammary tumor, and Olfactory epithelium;
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 [GENOMIC DNA] OF 1-108.
RX PubMed=3481036; DOI=10.1128/mcb.7.11.3929-3936.1987;
RA Roth W.W., Bragg P.W., Corrias M.V., Reddy N.S., Dholakia J.N., Wahba A.J.;
RT "Expression of a gene for mouse eucaryotic elongation factor Tu during
RT murine erythroleukemic cell differentiation.";
RL Mol. Cell. Biol. 7:3929-3936(1987).
RN [6]
RP NUCLEOTIDE SEQUENCE [MRNA] OF 1-94.
RX PubMed=3960725; DOI=10.1093/nar/14.5.2409;
RA Rao T.R., Slobin L.I.;
RT "Structure of the amino-terminal end of mammalian elongation factor Tu.";
RL Nucleic Acids Res. 14:2409-2409(1986).
RN [7]
RP PROTEIN SEQUENCE OF 6-30; 85-96; 135-146; 155-165; 248-290 AND 431-439, AND
RP IDENTIFICATION BY MASS SPECTROMETRY.
RC STRAIN=C57BL/6J, and OF1; TISSUE=Brain, and Hippocampus;
RA Lubec G., Kang S.U., Yang J.W., Zigmond M., Sunyer B., Chen W.-Q.;
RL Submitted (JAN-2009) to UniProtKB.
RN [8]
RP PROTEIN SEQUENCE OF 291-313 AND 372-376, AND ETHANOLAMINYLATION AT GLU-301
RP AND GLU-374.
RX PubMed=2569467; DOI=10.1016/s0021-9258(18)71682-7;
RA Whiteheart S.W., Shenbagarmurthi P., Chen L., Cotter R.J., Hart G.W.;
RT "Murine elongation factor 1 alpha (EF-1 alpha) is posttranslationally
RT modified by novel amide-linked ethanolamine-phosphoglycerol moieties.
RT Addition of ethanolamine-phosphoglycerol to specific glutamic acid residues
RT on EF-1 alpha.";
RL J. Biol. Chem. 264:14334-14341(1989).
RN [9]
RP ISGYLATION.
RX PubMed=16139798; DOI=10.1016/j.bbrc.2005.08.132;
RA Giannakopoulos N.V., Luo J.K., Papov V., Zou W., Lenschow D.J.,
RA Jacobs B.S., Borden E.C., Li J., Virgin H.W., Zhang D.E.;
RT "Proteomic identification of proteins conjugated to ISG15 in mouse and
RT human cells.";
RL Biochem. Biophys. Res. Commun. 336:496-506(2005).
RN [10]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Brain, Brown adipose tissue, Heart, Kidney, Liver, Lung, Pancreas,
RC Spleen, and Testis;
RX PubMed=21183079; DOI=10.1016/j.cell.2010.12.001;
RA Huttlin E.L., Jedrychowski M.P., Elias J.E., Goswami T., Rad R.,
RA Beausoleil S.A., Villen J., Haas W., Sowa M.E., Gygi S.P.;
RT "A tissue-specific atlas of mouse protein phosphorylation and expression.";
RL Cell 143:1174-1189(2010).
RN [11]
RP IDENTIFICATION BY MASS SPECTROMETRY, INTERACTION WITH IFIT1, AND
RP SUBCELLULAR LOCATION.
RX PubMed=19856081; DOI=10.1007/s11010-009-0289-9;
RA Li H.T., Su Y.P., Cheng T.M., Xu J.M., Liao J., Chen J.C., Ji C.Y.,
RA Ai G.P., Wang J.P.;
RT "The interaction between interferon-induced protein with tetratricopeptide
RT repeats-1 and eukaryotic elongation factor-1A.";
RL Mol. Cell. Biochem. 337:101-110(2010).
RN [12]
RP ACETYLATION [LARGE SCALE ANALYSIS] AT LYS-165; LYS-172; LYS-273; LYS-392
RP AND LYS-439, SUCCINYLATION [LARGE SCALE ANALYSIS] AT LYS-392, AND
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Embryonic fibroblast;
RX PubMed=23806337; DOI=10.1016/j.molcel.2013.06.001;
RA Park J., Chen Y., Tishkoff D.X., Peng C., Tan M., Dai L., Xie Z., Zhang Y.,
RA Zwaans B.M., Skinner M.E., Lombard D.B., Zhao Y.;
RT "SIRT5-mediated lysine desuccinylation impacts diverse metabolic
RT pathways.";
RL Mol. Cell 50:919-930(2013).
RN [13]
RP METHYLATION AT LYS-165.
RX PubMed=28108655; DOI=10.1093/nar/gkx002;
RA Malecki J., Aileni V.K., Ho A.Y., Schwarz J., Moen A., Soerensen V.,
RA Nilges B.S., Jakobsson M.E., Leidel S.A., Falnes P.O.;
RT "The novel lysine specific methyltransferase METTL21B affects mRNA
RT translation through inducible and dynamic methylation of Lys-165 in human
RT eukaryotic elongation factor 1 alpha (eEF1A).";
RL Nucleic Acids Res. 45:4370-4389(2017).
CC -!- FUNCTION: This protein promotes the GTP-dependent binding of aminoacyl-
CC tRNA to the A-site of ribosomes during protein biosynthesis. Plays a
CC role in the positive regulation of IFNG transcription in T-helper 1
CC cells as part of an IFNG promoter-binding complex with TXK and PARP1.
CC {ECO:0000250|UniProtKB:P68104}.
CC -!- ACTIVITY REGULATION: Inhibited by plitidepsin, a chemical compound
CC extracted from the ascidian Aplidium albicans.
CC {ECO:0000250|UniProtKB:P68104}.
CC -!- SUBUNIT: Found in a nuclear export complex with XPO5, EEF1A1, Ran and
CC aminoacylated tRNA. Interacts with PARP1 and TXK. Interacts with KARS1.
CC May interact with ERGIC2. Interacts with IFIT1 (via TPR repeats 4-7)
CC (By similarity). May interact with ERGIC2 (By similarity). Interacts
CC with IFIT1 (via TPR repeats 4-7) (PubMed:19856081). Interacts with
CC DLC1, facilitating distribution to the membrane periphery and ruffles
CC upon growth factor stimulation. Interacts with ZPR1; the interaction
CC occurs in a epidermal growth factor (EGF)-dependent manner (By
CC similarity). Interacts with PPP1R16B (By similarity). Interacts with
CC SPHK1 and SPHK2; both interactions increase SPHK1 and SPHK2 kinase
CC activity (By similarity). {ECO:0000250|UniProtKB:P68104,
CC ECO:0000269|PubMed:19856081}.
CC -!- INTERACTION:
CC P10126; Q01534: TSPY1; Xeno; NbExp=5; IntAct=EBI-773865, EBI-1973142;
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000269|PubMed:19856081}. Nucleus
CC {ECO:0000250|UniProtKB:P68104}. Nucleus, nucleolus
CC {ECO:0000250|UniProtKB:P68104}. Cell membrane
CC {ECO:0000250|UniProtKB:P68104}. Note=Colocalizes with DLC1 at actin-
CC rich regions in the cell periphery. Translocates together with ZPR1
CC from the cytoplasm to the nucleus and nucleolus after treatment with
CC mitogens. Localization at the cell membrane depends on EEF1A1
CC phosphorylation status and the presence of PPP1R16B.
CC {ECO:0000250|UniProtKB:P68104}.
CC -!- PTM: ISGylated. {ECO:0000269|PubMed:16139798}.
CC -!- PTM: Phosphorylated by TXK. Phosphorylation by PASK increases
CC translation efficiency. Phosphorylated by ROCK2.
CC {ECO:0000250|UniProtKB:P68104}.
CC -!- PTM: Trimethylated at Lys-79 by EEF1AKMT1 (By similarity). Methylated
CC at Lys-165 by EEF1AKMT3, methylation by EEF1AKMT3 is dynamic as well as
CC inducible by stress conditions, such as ER-stress, and plays a
CC regulatory role on mRNA translation (PubMed:28108655). Trimethylated at
CC Lys-318 by EEF1AKMT2 (By similarity). Mono-, di-, and trimethylated at
CC Lys-36 by EEF1AKMT4; trimethylated form is predominant. Methylation by
CC EEF1AKMT4 contributes to the fine-tuning of translation rates for a
CC subset of tRNAs (By similarity). Trimethylated at Gly-2 by METTL13.
CC Mono- and dimethylated at Lys-55 by METTL13; dimethylated form is
CC predominant (By similarity). {ECO:0000250|UniProtKB:P68104,
CC ECO:0000269|PubMed:28108655}.
CC -!- SIMILARITY: Belongs to the TRAFAC class translation factor GTPase
CC superfamily. Classic translation factor GTPase family. EF-Tu/EF-1A
CC subfamily. {ECO:0000305}.
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DR EMBL; M22432; AAA50406.1; -; mRNA.
DR EMBL; X13661; CAA31957.1; -; mRNA.
DR EMBL; AK032914; BAC28085.1; -; mRNA.
DR EMBL; AK076696; BAC36446.1; -; mRNA.
DR EMBL; AK081725; BAC38311.1; -; mRNA.
DR EMBL; AK083361; BAC38884.1; -; mRNA.
DR EMBL; BC004005; AAH04005.1; -; mRNA.
DR EMBL; BC004067; AAH04067.1; -; mRNA.
DR EMBL; BC005660; AAH05660.1; -; mRNA.
DR EMBL; BC018223; AAH18223.1; -; mRNA.
DR EMBL; BC018485; AAH18485.1; -; mRNA.
DR EMBL; BC083069; AAH83069.1; -; mRNA.
DR EMBL; M17878; AAA37538.1; -; Genomic_DNA.
DR EMBL; X03688; CAA27324.1; -; mRNA.
DR CCDS; CCDS40703.1; -.
DR PIR; S02114; EFMS1.
DR RefSeq; NP_034236.2; NM_010106.2.
DR AlphaFoldDB; P10126; -.
DR SMR; P10126; -.
DR BioGRID; 199385; 166.
DR DIP; DIP-46609N; -.
DR IntAct; P10126; 63.
DR MINT; P10126; -.
DR STRING; 10090.ENSMUSP00000042457; -.
DR iPTMnet; P10126; -.
DR PhosphoSitePlus; P10126; -.
DR SwissPalm; P10126; -.
DR SWISS-2DPAGE; P10126; -.
DR CPTAC; non-CPTAC-3787; -.
DR EPD; P10126; -.
DR jPOST; P10126; -.
DR PaxDb; P10126; -.
DR PeptideAtlas; P10126; -.
DR PRIDE; P10126; -.
DR ProteomicsDB; 275904; -.
DR TopDownProteomics; P10126; -.
DR Antibodypedia; 31353; 343 antibodies from 35 providers.
DR DNASU; 13627; -.
DR Ensembl; ENSMUST00000042235; ENSMUSP00000042457; ENSMUSG00000037742.
DR GeneID; 13627; -.
DR KEGG; mmu:13627; -.
DR UCSC; uc009qun.1; mouse.
DR CTD; 1915; -.
DR MGI; MGI:1096881; Eef1a1.
DR VEuPathDB; HostDB:ENSMUSG00000037742; -.
DR eggNOG; KOG0052; Eukaryota.
DR GeneTree; ENSGT00950000183029; -.
DR HOGENOM; CLU_007265_3_5_1; -.
DR InParanoid; P10126; -.
DR OMA; EMHHKSV; -.
DR OrthoDB; 1150082at2759; -.
DR PhylomeDB; P10126; -.
DR TreeFam; TF300304; -.
DR Reactome; R-MMU-156842; Eukaryotic Translation Elongation.
DR Reactome; R-MMU-3371511; HSF1 activation.
DR Reactome; R-MMU-6798695; Neutrophil degranulation.
DR Reactome; R-MMU-8876725; Protein methylation.
DR BioGRID-ORCS; 13627; 26 hits in 60 CRISPR screens.
DR ChiTaRS; Eef1a1; mouse.
DR PRO; PR:P10126; -.
DR Proteomes; UP000000589; Chromosome 9.
DR RNAct; P10126; protein.
DR Bgee; ENSMUSG00000037742; Expressed in epiblast (generic) and 76 other tissues.
DR ExpressionAtlas; P10126; baseline and differential.
DR Genevisible; P10126; MM.
DR GO; GO:0030864; C:cortical actin cytoskeleton; ISO:MGI.
DR GO; GO:0005737; C:cytoplasm; IDA:UniProtKB.
DR GO; GO:0005829; C:cytosol; ISO:MGI.
DR GO; GO:0043209; C:myelin sheath; HDA:UniProtKB.
DR GO; GO:0005730; C:nucleolus; ISS:UniProtKB.
DR GO; GO:0005634; C:nucleus; ISS:UniProtKB.
DR GO; GO:0005886; C:plasma membrane; IDA:MGI.
DR GO; GO:0032587; C:ruffle membrane; ISO:MGI.
DR GO; GO:0005516; F:calmodulin binding; IDA:CAFA.
DR GO; GO:0005525; F:GTP binding; IEA:UniProtKB-KW.
DR GO; GO:0003924; F:GTPase activity; IBA:GO_Central.
DR GO; GO:1901363; F:heterocyclic compound binding; ISO:MGI.
DR GO; GO:0042802; F:identical protein binding; ISO:MGI.
DR GO; GO:0019900; F:kinase binding; ISO:MGI.
DR GO; GO:0003729; F:mRNA binding; ISO:MGI.
DR GO; GO:0019901; F:protein kinase binding; ISO:MGI.
DR GO; GO:0003746; F:translation elongation factor activity; IBA:GO_Central.
DR GO; GO:0000049; F:tRNA binding; ISO:MGI.
DR GO; GO:0007568; P:aging; IEA:Ensembl.
DR GO; GO:0071364; P:cellular response to epidermal growth factor stimulus; ISS:UniProtKB.
DR GO; GO:1990090; P:cellular response to nerve growth factor stimulus; IEA:Ensembl.
DR GO; GO:0071466; P:cellular response to xenobiotic stimulus; IEA:Ensembl.
DR GO; GO:1903427; P:negative regulation of reactive oxygen species biosynthetic process; ISO:MGI.
DR GO; GO:0010942; P:positive regulation of cell death; ISO:MGI.
DR GO; GO:0010976; P:positive regulation of neuron projection development; ISO:MGI.
DR GO; GO:1900022; P:regulation of D-erythro-sphingosine kinase activity; ISS:UniProtKB.
DR GO; GO:0006412; P:translation; IBA:GO_Central.
DR GO; GO:0006414; P:translational elongation; IBA:GO_Central.
DR Gene3D; 3.40.50.300; -; 1.
DR HAMAP; MF_00118_A; EF_Tu_A; 1.
DR InterPro; IPR004161; EFTu-like_2.
DR InterPro; IPR031157; G_TR_CS.
DR InterPro; IPR027417; P-loop_NTPase.
DR InterPro; IPR000795; T_Tr_GTP-bd_dom.
DR InterPro; IPR009000; Transl_B-barrel_sf.
DR InterPro; IPR009001; Transl_elong_EF1A/Init_IF2_C.
DR InterPro; IPR004539; Transl_elong_EF1A_euk/arc.
DR InterPro; IPR004160; Transl_elong_EFTu/EF1A_C.
DR Pfam; PF00009; GTP_EFTU; 1.
DR Pfam; PF03144; GTP_EFTU_D2; 1.
DR Pfam; PF03143; GTP_EFTU_D3; 1.
DR PRINTS; PR00315; ELONGATNFCT.
DR SUPFAM; SSF50447; SSF50447; 1.
DR SUPFAM; SSF50465; SSF50465; 1.
DR SUPFAM; SSF52540; SSF52540; 1.
DR TIGRFAMs; TIGR00483; EF-1_alpha; 1.
DR PROSITE; PS00301; G_TR_1; 1.
DR PROSITE; PS51722; G_TR_2; 1.
PE 1: Evidence at protein level;
KW Acetylation; Cell membrane; Cytoplasm; Direct protein sequencing;
KW Elongation factor; GTP-binding; Membrane; Methylation; Nucleotide-binding;
KW Nucleus; Phosphoprotein; Protein biosynthesis; Reference proteome;
KW Ubl conjugation.
FT INIT_MET 1
FT /note="Removed"
FT /evidence="ECO:0000250|UniProtKB:P68104"
FT CHAIN 2..462
FT /note="Elongation factor 1-alpha 1"
FT /id="PRO_0000090886"
FT DOMAIN 5..242
FT /note="tr-type G"
FT REGION 14..21
FT /note="G1"
FT /evidence="ECO:0000250"
FT REGION 70..74
FT /note="G2"
FT /evidence="ECO:0000250"
FT REGION 91..94
FT /note="G3"
FT /evidence="ECO:0000250"
FT REGION 153..156
FT /note="G4"
FT /evidence="ECO:0000250"
FT REGION 194..196
FT /note="G5"
FT /evidence="ECO:0000250"
FT BINDING 14..21
FT /ligand="GTP"
FT /ligand_id="ChEBI:CHEBI:37565"
FT /evidence="ECO:0000250"
FT BINDING 91..95
FT /ligand="GTP"
FT /ligand_id="ChEBI:CHEBI:37565"
FT /evidence="ECO:0000250"
FT BINDING 153..156
FT /ligand="GTP"
FT /ligand_id="ChEBI:CHEBI:37565"
FT /evidence="ECO:0000250"
FT MOD_RES 2
FT /note="N,N,N-trimethylglycine"
FT /evidence="ECO:0000250|UniProtKB:P68104"
FT MOD_RES 36
FT /note="N6,N6,N6-trimethyllysine; alternate"
FT /evidence="ECO:0000250|UniProtKB:P68104"
FT MOD_RES 36
FT /note="N6,N6-dimethyllysine; alternate"
FT /evidence="ECO:0000250|UniProtKB:P68104"
FT MOD_RES 36
FT /note="N6-methyllysine; alternate"
FT /evidence="ECO:0000250|UniProtKB:P68104"
FT MOD_RES 55
FT /note="N6,N6-dimethyllysine"
FT /evidence="ECO:0000250|UniProtKB:P68104"
FT MOD_RES 79
FT /note="N6,N6,N6-trimethyllysine; by EEF1AKMT1"
FT /evidence="ECO:0000250|UniProtKB:P68104"
FT MOD_RES 165
FT /note="N6,N6,N6-trimethyllysine; alternate; by EEF1AKMT3"
FT /evidence="ECO:0000269|PubMed:28108655"
FT MOD_RES 165
FT /note="N6,N6-dimethyllysine; alternate; by EEF1AKMT3"
FT /evidence="ECO:0000250|UniProtKB:P68104"
FT MOD_RES 165
FT /note="N6-acetyllysine; alternate"
FT /evidence="ECO:0007744|PubMed:23806337"
FT MOD_RES 165
FT /note="N6-methyllysine; alternate; by EEF1AKMT3"
FT /evidence="ECO:0000250|UniProtKB:P68104"
FT MOD_RES 172
FT /note="N6-acetyllysine"
FT /evidence="ECO:0007744|PubMed:23806337"
FT MOD_RES 273
FT /note="N6-acetyllysine"
FT /evidence="ECO:0007744|PubMed:23806337"
FT MOD_RES 300
FT /note="Phosphoserine; by TGFBR1"
FT /evidence="ECO:0000250|UniProtKB:P68104"
FT MOD_RES 301
FT /note="5-glutamyl glycerylphosphorylethanolamine"
FT /evidence="ECO:0000269|PubMed:2569467"
FT MOD_RES 318
FT /note="N6,N6,N6-trimethyllysine; by EEF1AKMT2"
FT /evidence="ECO:0000250|UniProtKB:P68104"
FT MOD_RES 374
FT /note="5-glutamyl glycerylphosphorylethanolamine"
FT /evidence="ECO:0000269|PubMed:2569467"
FT MOD_RES 392
FT /note="N6-acetyllysine; alternate"
FT /evidence="ECO:0007744|PubMed:23806337"
FT MOD_RES 392
FT /note="N6-succinyllysine; alternate"
FT /evidence="ECO:0007744|PubMed:23806337"
FT MOD_RES 432
FT /note="Phosphothreonine; by PASK"
FT /evidence="ECO:0000250|UniProtKB:P68104"
FT MOD_RES 439
FT /note="N6-acetyllysine"
FT /evidence="ECO:0007744|PubMed:23806337"
FT CONFLICT 7
FT /note="H -> R (in Ref. 5; AAA37538)"
FT /evidence="ECO:0000305"
FT CONFLICT 15
FT /note="H -> L (in Ref. 5; AAA37538)"
FT /evidence="ECO:0000305"
FT CONFLICT 23
FT /note="T -> S (in Ref. 5; AAA37538)"
FT /evidence="ECO:0000305"
FT CONFLICT 77..78
FT /note="LW -> QR (in Ref. 2; CAA31957)"
FT /evidence="ECO:0000305"
FT CONFLICT 83
FT /note="S -> A (in Ref. 6; CAA27324)"
FT /evidence="ECO:0000305"
FT CONFLICT 91..92
FT /note="DA -> ES (in Ref. 2; CAA31957)"
FT /evidence="ECO:0000305"
FT CONFLICT 108
FT /note="Q -> R (in Ref. 5; AAA37538)"
FT /evidence="ECO:0000305"
FT CONFLICT 156
FT /note="D -> G (in Ref. 3; BAC28085)"
FT /evidence="ECO:0000305"
FT CONFLICT 222
FT /note="S -> H (in Ref. 1; AAA50406)"
FT /evidence="ECO:0000305"
FT CONFLICT 224..226
FT /note="SGT -> VAP (in Ref. 2; CAA31957)"
FT /evidence="ECO:0000305"
FT CONFLICT 225
FT /note="G -> D (in Ref. 4; AAH04005)"
FT /evidence="ECO:0000305"
FT CONFLICT 239
FT /note="Missing (in Ref. 2; CAA31957)"
FT /evidence="ECO:0000305"
FT CONFLICT 350
FT /note="P -> T (in Ref. 3; BAC36446)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 462 AA; 50114 MW; 71072871DE7405DC CRC64;
MGKEKTHINI VVIGHVDSGK STTTGHLIYK CGGIDKRTIE KFEKEAAEMG KGSFKYAWVL
DKLKAERERG ITIDISLWKF ETSKYYVTII DAPGHRDFIK NMITGTSQAD CAVLIVAAGV
GEFEAGISKN GQTREHALLA YTLGVKQLIV GVNKMDSTEP PYSQKRYEEI VKEVSTYIKK
IGYNPDTVAF VPISGWNGDN MLEPSANMPW FKGWKVTRKD GSASGTTLLE ALDCILPPTR
PTDKPLRLPL QDVYKIGGIG TVPVGRVETG VLKPGMVVTF APVNVTTEVK SVEMHHEALS
EALPGDNVGF NVKNVSVKDV RRGNVAGDSK NDPPMEAAGF TAQVIILNHP GQISAGYAPV
LDCHTAHIAC KFAELKEKID RRSGKKLEDG PKFLKSGDAA IVDMVPGKPM CVESFSDYPP
LGRFAVRDMR QTVAVGVIKA VDKKAAGAGK VTKSAQKAQK AK
