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 22-APR-2020, entry version 214. 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; 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; 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. With PARP1 CC and TXK, forms a complex that acts as a T helper 1 (Th1) cell-specific CC transcription factor and binds the promoter of IFN-gamma to directly CC regulate its transcription, and is thus involved importantly in Th1 CC cytokine production. {ECO:0000250|UniProtKB:P68104}. CC -!- SUBUNIT: Found in a nuclear export complex with XPO5, EEF1A1, Ran and CC aminoacylated tRNA. Interacts with PARP1, TXK, XPO5 and KARS1. May CC interact with ERGIC2 (By similarity). Interacts with IFIT1 (via TPR CC repeats 4-7) (PubMed:19856081). Interacts with DLC1, facilitating CC distribution to the membrane periphery and ruffles upon growth factor CC stimulation. Interacts with ZPR1; the interaction occurs in a epidermal CC growth factor (EGF)-dependent manner (By similarity). Interacts with CC PPP1R16B (By similarity). Interacts with SPHK1 and SPHK2; both CC interactions increase SPHK1 and SPHK2 kinase activity (By similarity). CC {ECO:0000250|UniProtKB:P68104, 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 EEF1AKNMT. CC Mono- and dimethylated at Lys-55 by EEF1AKNMT; 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}. 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 SMR; P10126; -. DR BioGrid; 199385; 63. DR DIP; DIP-46609N; -. DR IntAct; P10126; 68. 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 TopDownProteomics; P10126; -. 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 eggNOG; KOG0052; Eukaryota. DR eggNOG; COG5256; LUCA. DR GeneTree; ENSGT00950000183029; -. DR HOGENOM; CLU_007265_3_5_1; -. DR InParanoid; P10126; -. DR KO; K03231; -. DR OMA; ICAINKM; -. 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 ChiTaRS; Eef1a1; mouse. DR PRO; PR:P10126; -. DR Proteomes; UP000000589; Chromosome 9. DR RNAct; P10126; protein. DR Bgee; ENSMUSG00000037742; Expressed in female gonad and 62 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:0008144; F:drug binding; ISO:MGI. DR GO; GO:0005525; F:GTP binding; IEA:UniProtKB-KW. DR GO; GO:0003924; F:GTPase activity; IBA:GO_Central. 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:0071364; P:cellular response to epidermal growth factor stimulus; ISS:UniProtKB. 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 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; TF_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 NP_BIND 14..21 FT /note="GTP" FT /evidence="ECO:0000250" FT NP_BIND 91..95 FT /note="GTP" FT /evidence="ECO:0000250" FT NP_BIND 153..156 FT /note="GTP" FT /evidence="ECO:0000250" 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 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:0000244|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:0000244|PubMed:23806337" FT MOD_RES 273 FT /note="N6-acetyllysine" FT /evidence="ECO:0000244|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:0000244|PubMed:23806337" FT MOD_RES 392 FT /note="N6-succinyllysine; alternate" FT /evidence="ECO:0000244|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:0000244|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 //