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 24-JUL-2024, entry version 236. DE RecName: Full=Elongation factor 1-alpha 1; DE Short=EF-1-alpha-1; DE EC=3.6.5.- {ECO:0000250|UniProtKB:P68104}; 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: Translation elongation factor that catalyzes the GTP- CC dependent binding of aminoacyl-tRNA (aa-tRNA) to the A-site of CC ribosomes during the elongation phase of protein synthesis. Base CC pairing between the mRNA codon and the aa-tRNA anticodon promotes GTP CC hydrolysis, releasing the aa-tRNA from EEF1A1 and allowing its CC accommodation into the ribosome. The growing protein chain is CC subsequently transferred from the P-site peptidyl tRNA to the A-site CC aa-tRNA, extending it by one amino acid through ribosome-catalyzed CC peptide bond formation. Also plays a role in the positive regulation of CC IFNG transcription in T-helper 1 cells as part of an IFNG promoter- CC binding complex with TXK and PARP1. {ECO:0000250|UniProtKB:P68104}. CC -!- CATALYTIC ACTIVITY: CC Reaction=GTP + H2O = GDP + H(+) + phosphate; Xref=Rhea:RHEA:19669, CC ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:37565, CC ChEBI:CHEBI:43474, ChEBI:CHEBI:58189; CC Evidence={ECO:0000250|UniProtKB:P68104}; CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:19670; CC Evidence={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. Interacts with KARS1. May CC interact with ERGIC2. Interacts with IFIT1 (via TPR repeats 4-7) (By CC similarity). May interact with ERGIC2 (By similarity). Interacts with CC IFIT1 (via TPR repeats 4-7) (PubMed:19856081). Interacts with DLC1, CC facilitating distribution to the membrane periphery and ruffles upon CC growth factor stimulation. Interacts with ZPR1; the interaction occurs CC in a epidermal growth factor (EGF)-dependent manner (By similarity). CC Interacts with PPP1R16B (By similarity). Interacts with SPHK1 and CC SPHK2; both interactions increase SPHK1 and SPHK2 kinase activity (By CC 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:0000250|UniProtKB:P68104}. CC -!- PTM: Phosphorylated by TXK. Phosphorylation by PASK increases CC translation efficiency. Phosphorylated by ROCK2. Phosphorylation by CC TGFBR1 inhibits translation elongation. {ECO:0000250|UniProtKB:P68104}. CC -!- PTM: Trimethylated at Lys-79 by EEF1AKMT1. Methylated at Lys-165 by CC EEF1AKMT3, methylation by EEF1AKMT3 is dynamic as well as inducible by CC stress conditions, such as ER-stress, and plays a regulatory role on CC mRNA translation. Trimethylated at Lys-318 by EEF1AKMT2. Mono-, di-, CC and trimethylated at Lys-36 by EEF1AKMT4; trimethylated form is CC predominant. Methylation by EEF1AKMT4 contributes to the fine-tuning of CC translation rates for a subset of tRNAs. Trimethylated at Gly-2 by CC METTL13. Mono- and dimethylated at Lys-55 by METTL13; dimethylated form CC is predominant. {ECO:0000250|UniProtKB:P68104}. CC -!- PTM: Ubiquitinated at Lys-385 by RNF14 in response to ribosome CC collisions (ribosome stalling), leading to its degradation by the CC proteasome and rescue of stalled ribosomes. CC {ECO:0000250|UniProtKB:P68104}. 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}. 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; 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; 171. DR DIP; DIP-46609N; -. DR IntAct; P10126; 63. DR MINT; P10126; -. DR STRING; 10090.ENSMUSP00000042457; -. DR GlyGen; P10126; 1 site, 1 O-linked glycan (1 site). DR iPTMnet; P10126; -. DR MetOSite; P10126; -. DR PhosphoSitePlus; P10126; -. DR SwissPalm; P10126; -. DR CPTAC; non-CPTAC-3787; -. DR jPOST; P10126; -. DR PaxDb; 10090-ENSMUSP00000042457; -. DR PeptideAtlas; P10126; -. DR ProteomicsDB; 275904; -. DR Pumba; P10126; -. DR TopDownProteomics; P10126; -. DR Antibodypedia; 31353; 358 antibodies from 36 providers. DR DNASU; 13627; -. DR Ensembl; ENSMUST00000042235.15; ENSMUSP00000042457.9; ENSMUSG00000037742.15. DR GeneID; 13627; -. DR KEGG; mmu:13627; -. DR UCSC; uc009qun.1; mouse. DR AGR; MGI:1096881; -. 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; 5477300at2759; -. 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 65 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 79 other cell types or tissues. DR ExpressionAtlas; P10126; baseline and differential. DR GO; GO:0005737; C:cytoplasm; IDA:UniProtKB. 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:0005516; F:calmodulin binding; IDA:CAFA. DR GO; GO:0005525; F:GTP binding; IEA:UniProtKB-KW. DR GO; GO:0003924; F:GTPase activity; ISS:UniProtKB. DR GO; GO:1901363; F:heterocyclic compound binding; ISO:MGI. DR GO; GO:0042802; F:identical protein binding; ISO:MGI. DR GO; GO:0003729; F:mRNA binding; ISO:MGI. DR GO; GO:0003746; F:translation elongation factor activity; ISS:UniProtKB. DR GO; GO:0071364; P:cellular response to epidermal growth factor stimulus; ISS:UniProtKB. 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; ISS:UniProtKB. DR CDD; cd01883; EF1_alpha; 1. DR CDD; cd03693; EF1_alpha_II; 1. DR CDD; cd03705; EF1_alpha_III; 1. DR Gene3D; 3.40.50.300; P-loop containing nucleotide triphosphate hydrolases; 1. DR Gene3D; 2.40.30.10; Translation factors; 2. 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; IPR050100; TRAFAC_GTPase_members. 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 NCBIfam; TIGR00483; EF-1_alpha; 1. DR PANTHER; PTHR23115:SF222; ELONGATION FACTOR 1-ALPHA 1-RELATED; 1. DR PANTHER; PTHR23115; TRANSLATION FACTOR; 1. 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; SSF50465; EF-Tu/eEF-1alpha/eIF2-gamma C-terminal domain; 1. DR SUPFAM; SSF52540; P-loop containing nucleoside triphosphate hydrolases; 1. DR SUPFAM; SSF50447; Translation proteins; 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; Hydrolase; Isopeptide bond; Membrane; KW Methylation; Nucleotide-binding; Nucleus; Phosphoprotein; KW Protein biosynthesis; Reference proteome; 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:0000255" FT REGION 70..74 FT /note="G2" FT /evidence="ECO:0000255" FT REGION 91..94 FT /note="G3" FT /evidence="ECO:0000255" FT REGION 153..156 FT /note="G4" FT /evidence="ECO:0000255" FT REGION 194..196 FT /note="G5" FT /evidence="ECO:0000255" FT BINDING 14..21 FT /ligand="GTP" FT /ligand_id="ChEBI:CHEBI:37565" FT /evidence="ECO:0000250|UniProtKB:P68105" FT BINDING 153..156 FT /ligand="GTP" FT /ligand_id="ChEBI:CHEBI:37565" FT /evidence="ECO:0000250|UniProtKB:P68105" FT BINDING 194..196 FT /ligand="GTP" FT /ligand_id="ChEBI:CHEBI:37565" FT /evidence="ECO:0000250|UniProtKB:P68105" 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 CROSSLNK 385 FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with FT G-Cter in ubiquitin)" FT /evidence="ECO:0000250|UniProtKB:P68104" 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 //