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 07-JAN-2015, entry version 161. 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; OC Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Sciurognathi; OC Muroidea; Muridae; 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 RT factor 4A and its expression during differentiation of murine RT erythroleukemia 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 RT alpha) 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., RA Davis M.J., Wilming L.G., Aidinis V., Allen J.E., RA Ambesi-Impiombato A., Apweiler R., Aturaliya R.N., Bailey T.L., RA Bansal M., Baxter L., Beisel K.W., Bersano T., Bono H., Chalk A.M., RA Chiu K.P., Choudhary V., Christoffels A., Clutterbuck D.R., RA Crowe M.L., Dalla E., Dalrymple B.P., de Bono B., Della Gatta G., RA di Bernardo D., Down T., Engstrom P., Fagiolini M., Faulkner G., RA Fletcher C.F., Fukushima T., Furuno M., Futaki S., Gariboldi M., RA Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E., RA Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N., RA Hill D., Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T., RA Jakt M., Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H., RA Kitano H., Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K., RA Kurochkin I.V., Lareau L.F., Lazarevic D., Lipovich L., Liu J., RA Liuni S., McWilliam S., Madan Babu M., Madera M., Marchionni L., RA Matsuda H., Matsuzawa S., Miki H., Mignone F., Miyake S., Morris K., RA Mottagui-Tabar S., Mulder N., Nakano N., Nakauchi H., Ng P., RA Nilsson R., Nishiguchi S., Nishikawa S., Nori F., Ohara O., RA Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G., Pesole G., RA Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z., Ringwald M., RA 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., RA Sperling S., Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K., RA Tammoja K., Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A., RA Ueda H.R., van Nimwegen E., Verardo R., Wei C.L., Yagi K., RA Yamanishi H., Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C., RA Grimmond S.M., Teasdale R.D., Liu E.T., Brusic V., Quackenbush J., RA Wahlestedt C., Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y., RA Fukuda S., Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T., RA Iida J., Imamura K., Itoh M., Kato T., Kawaji H., Kawagashira N., RA Kawashima T., Kojima M., Kondo S., Konno H., Nakano K., Ninomiya N., RA Nishio T., Okada M., Plessy C., Shibata K., Shiraki T., Suzuki S., RA Tagami M., Waki K., Watahiki A., Okamura-Oho Y., Suzuki H., Kawai J., RA 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 RT project: 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; RA Roth W.W., Bragg P.W., Corrias M.V., Reddy N.S., Dholakia J.N., RA 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 RT 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 RP 431-439, AND IDENTIFICATION BY MASS SPECTROMETRY. RC STRAIN=C57BL/6, 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 RP GLU-301 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 RT residues 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, 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 RT tetratricopeptide repeats-1 and eukaryotic elongation factor-1A."; RL Mol. Cell. Biochem. 337:101-110(2010). RN [11] RP ACETYLATION [LARGE SCALE ANALYSIS] AT LYS-165; LYS-172; LYS-273; RP LYS-392 AND LYS-439, SUCCINYLATION [LARGE SCALE ANALYSIS] AT LYS-392, RP AND 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., RA Zhang Y., 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). CC -!- FUNCTION: This protein promotes the GTP-dependent binding of CC aminoacyl-tRNA to the A-site of ribosomes during protein CC biosynthesis. With PARP1 and TXK, forms a complex that acts as a T CC helper 1 (Th1) cell-specific transcription factor and binds the CC promoter of IFN-gamma to directly regulate its transcription, and CC is thus involved importantly in Th1 cytokine production (By CC similarity). {ECO:0000250}. CC -!- SUBUNIT: Found in a nuclear export complex with XPO5, EEF1A1, Ran CC and aminoacylated tRNA. Interacts with PARP1, TXK, XPO5 and KARS CC (By similarity). May interact with ERGIC2 (By similarity). CC Interacts with DLC1, facilitating distribution to the membrane CC periphery and ruffles upon growth factor stimulation (By CC similarity). Interacts with ZPR1; the interaction occurs in a CC epidermal growth factor (EGF)-dependent manner (By similarity). CC Interacts with IFIT1 (via TPR repeats 4-7). {ECO:0000250, CC ECO:0000269|PubMed:19856081}. CC -!- INTERACTION: CC Q01534:TSPY1 (xeno); NbExp=5; IntAct=EBI-773865, EBI-1973142; CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000269|PubMed:19856081}. CC Nucleus {ECO:0000250}. Nucleus, nucleolus {ECO:0000250}. CC Note=Colocalizes with DLC1 at actin-rich regions in the cell CC periphery. Translocates together with ZPR1 from the cytoplasm to CC the nucleus and nucleolus after treatment with mitogens (By CC similarity). {ECO:0000250}. CC -!- PTM: ISGylated. {ECO:0000269|PubMed:16139798}. CC -!- PTM: Phosphorylated by TXK. Phosphorylation by PASK increases CC translation efficiency (By similarity). {ECO:0000250}. 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 -!- SIMILARITY: Contains 1 tr-type G (guanine nucleotide-binding) CC domain. {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 UniGene; Mm.138471; -. DR UniGene; Mm.335315; -. DR UniGene; Mm.360075; -. DR UniGene; Mm.391071; -. DR UniGene; Mm.485669; -. DR UniGene; Mm.491424; -. DR ProteinModelPortal; P10126; -. DR SMR; P10126; 4-455. DR BioGrid; 199385; 13. DR DIP; DIP-46609N; -. DR IntAct; P10126; 25. DR MINT; MINT-1862449; -. DR PhosphoSite; P10126; -. DR SWISS-2DPAGE; P10126; -. DR MaxQB; P10126; -. DR PaxDb; P10126; -. DR PRIDE; 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; COG5256; -. DR HOGENOM; HOG000229291; -. DR HOVERGEN; HBG000179; -. DR InParanoid; P10126; -. DR KO; K03231; -. DR OMA; AIRDMGM; -. DR OrthoDB; EOG7NKKK3; -. DR PhylomeDB; P10126; -. DR TreeFam; TF300304; -. DR Reactome; REACT_225256; HSF1 activation. DR Reactome; REACT_232254; Eukaryotic Translation Elongation. DR Reactome; REACT_253640; Peptide chain elongation. DR NextBio; 284304; -. DR PRO; PR:P10126; -. DR Proteomes; UP000000589; Chromosome 9. DR Bgee; P10126; -. DR ExpressionAtlas; P10126; baseline. DR Genevestigator; P10126; -. DR GO; GO:0005737; C:cytoplasm; IDA:UniProtKB. DR GO; GO:0005615; C:extracellular space; IEA:Ensembl. DR GO; GO:0070062; C:extracellular vesicular exosome; IEA:Ensembl. 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:0005525; F:GTP binding; IEA:UniProtKB-KW. DR GO; GO:0003924; F:GTPase activity; IEA:InterPro. DR GO; GO:0044822; F:poly(A) RNA binding; IEA:Ensembl. DR GO; GO:0003746; F:translation elongation factor activity; IEA:UniProtKB-KW. DR GO; GO:0071364; P:cellular response to epidermal growth factor stimulus; ISS:UniProtKB. DR Gene3D; 3.40.50.300; -; 1. DR HAMAP; MF_00118_A; EF_Tu_A; 1. DR InterPro; IPR000795; EF_GTP-bd_dom. DR InterPro; IPR027417; P-loop_NTPase. DR InterPro; IPR009000; Transl_B-barrel. DR InterPro; IPR009001; Transl_elong_EF1A/Init_IF2_C. DR InterPro; IPR004539; Transl_elong_EF1A_euk/arc. DR InterPro; IPR004161; Transl_elong_EFTu/EF1A_2. 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; Complete proteome; Cytoplasm; Direct protein sequencing; KW Elongation factor; GTP-binding; Methylation; Nucleotide-binding; KW Nucleus; Phosphoprotein; Protein biosynthesis; Reference proteome; KW Ubl conjugation. FT CHAIN 1 462 Elongation factor 1-alpha 1. FT /FTId=PRO_0000090886. FT DOMAIN 5 242 tr-type G. FT NP_BIND 14 21 GTP. {ECO:0000250}. FT NP_BIND 91 95 GTP. {ECO:0000250}. FT NP_BIND 153 156 GTP. {ECO:0000250}. FT REGION 14 21 G1. {ECO:0000250}. FT REGION 70 74 G2. {ECO:0000250}. FT REGION 91 94 G3. {ECO:0000250}. FT REGION 153 156 G4. {ECO:0000250}. FT REGION 194 196 G5. {ECO:0000250}. FT MOD_RES 36 36 N6,N6,N6-trimethyllysine. {ECO:0000250}. FT MOD_RES 55 55 N6,N6-dimethyllysine. {ECO:0000250}. FT MOD_RES 79 79 N6,N6,N6-trimethyllysine. {ECO:0000250}. FT MOD_RES 165 165 N6,N6-dimethyllysine; alternate. FT {ECO:0000250}. FT MOD_RES 165 165 N6-acetyllysine; alternate. FT {ECO:0000269|PubMed:23806337}. FT MOD_RES 172 172 N6-acetyllysine. FT {ECO:0000269|PubMed:23806337}. FT MOD_RES 273 273 N6-acetyllysine. FT {ECO:0000269|PubMed:23806337}. FT MOD_RES 300 300 Phosphoserine; by TGFBR1. {ECO:0000250}. FT MOD_RES 301 301 5-glutamyl FT glycerylphosphorylethanolamine. FT {ECO:0000269|PubMed:2569467}. FT MOD_RES 318 318 N6,N6,N6-trimethyllysine. {ECO:0000250}. FT MOD_RES 374 374 5-glutamyl FT glycerylphosphorylethanolamine. FT {ECO:0000269|PubMed:2569467}. FT MOD_RES 392 392 N6-acetyllysine; alternate. FT {ECO:0000269|PubMed:23806337}. FT MOD_RES 392 392 N6-succinyllysine; alternate. FT {ECO:0000269|PubMed:23806337}. FT MOD_RES 432 432 Phosphothreonine; by PASK. {ECO:0000250}. FT MOD_RES 439 439 N6-acetyllysine. FT {ECO:0000269|PubMed:23806337}. FT CONFLICT 7 7 H -> R (in Ref. 5; AAA37538). FT {ECO:0000305}. FT CONFLICT 15 15 H -> L (in Ref. 5; AAA37538). FT {ECO:0000305}. FT CONFLICT 23 23 T -> S (in Ref. 5; AAA37538). FT {ECO:0000305}. FT CONFLICT 77 78 LW -> QR (in Ref. 2; CAA31957). FT {ECO:0000305}. FT CONFLICT 83 83 S -> A (in Ref. 6; CAA27324). FT {ECO:0000305}. FT CONFLICT 91 92 DA -> ES (in Ref. 2; CAA31957). FT {ECO:0000305}. FT CONFLICT 108 108 Q -> R (in Ref. 5; AAA37538). FT {ECO:0000305}. FT CONFLICT 156 156 D -> G (in Ref. 3; BAC28085). FT {ECO:0000305}. FT CONFLICT 222 222 S -> H (in Ref. 1; AAA50406). FT {ECO:0000305}. FT CONFLICT 224 226 SGT -> VAP (in Ref. 2; CAA31957). FT {ECO:0000305}. FT CONFLICT 225 225 G -> D (in Ref. 4; AAH04005). FT {ECO:0000305}. FT CONFLICT 239 239 Missing (in Ref. 2; CAA31957). FT {ECO:0000305}. FT CONFLICT 350 350 P -> T (in Ref. 3; BAC36446). FT {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 //