ID EF11_MOUSE STANDARD; PRT; 462 AA. AC P10126; Q61511; Q6ZWN2; Q8BMB8; Q8BVS8; Q99KU5; DT 01-MAR-1989 (Rel. 10, Created) DT 25-OCT-2004 (Rel. 45, Last sequence update) DT 25-OCT-2004 (Rel. 45, Last annotation update) DE Elongation factor 1-alpha 1 (EF-1-alpha-1) (Elongation factor 1 A-1) DE (eEF1A-1) (Elongation factor Tu) (EF-Tu). GN Name=Eef1a1; Synonyms=Eef1a; OS Mus musculus (Mouse). OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; OC Mammalia; Eutheria; Rodentia; Sciurognathi; Muridae; Murinae; Mus. OX NCBI_TaxID=10090; RN [1] RP SEQUENCE FROM N.A. RX MEDLINE=89108007; 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 SEQUENCE FROM N.A. RX MEDLINE=89098401; PubMed=2911475; 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 SEQUENCE FROM N.A. RC STRAIN=C57BL/6J; TISSUE=Head, Testis, and Thymus; RX MEDLINE=22354683; PubMed=12466851; DOI=10.1038/nature01266; RA Okazaki Y., Furuno M., Kasukawa T., Adachi J., Bono H., Kondo S., RA Nikaido I., Osato N., Saito R., Suzuki H., Yamanaka I., Kiyosawa H., RA Yagi K., Tomaru Y., Hasegawa Y., Nogami A., Schonbach C., Gojobori T., RA Baldarelli R., Hill D.P., Bult C., Hume D.A., Quackenbush J., RA Schriml L.M., Kanapin A., Matsuda H., Batalov S., Beisel K.W., RA Blake J.A., Bradt D., Brusic V., Chothia C., Corbani L.E., Cousins S., RA Dalla E., Dragani T.A., Fletcher C.F., Forrest A., Frazer K.S., RA Gaasterland T., Gariboldi M., Gissi C., Godzik A., Gough J., RA Grimmond S., Gustincich S., Hirokawa N., Jackson I.J., Jarvis E.D., RA Kanai A., Kawaji H., Kawasawa Y., Kedzierski R.M., King B.L., RA Konagaya A., Kurochkin I.V., Lee Y., Lenhard B., Lyons P.A., RA Maglott D.R., Maltais L., Marchionni L., McKenzie L., Miki H., RA Nagashima T., Numata K., Okido T., Pavan W.J., Pertea G., Pesole G., RA Petrovsky N., Pillai R., Pontius J.U., Qi D., Ramachandran S., RA Ravasi T., Reed J.C., Reed D.J., Reid J., Ring B.Z., Ringwald M., RA Sandelin A., Schneider C., Semple C.A., Setou M., Shimada K., RA Sultana R., Takenaka Y., Taylor M.S., Teasdale R.D., Tomita M., RA Verardo R., Wagner L., Wahlestedt C., Wang Y., Watanabe Y., Wells C., RA Wilming L.G., Wynshaw-Boris A., Yanagisawa M., Yang I., Yang L., RA Yuan Z., Zavolan M., Zhu Y., Zimmer A., Carninci P., Hayatsu N., RA Hirozane-Kishikawa T., Konno H., Nakamura M., Sakazume N., Sato K., RA Shiraki T., Waki K., Kawai J., Aizawa K., Arakawa T., Fukuda S., RA Hara A., Hashizume W., Imotani K., Ishii Y., Itoh M., Kagawa I., RA Miyazaki A., Sakai K., Sasaki D., Shibata K., Shinagawa A., RA Yasunishi A., Yoshino M., Waterston R., Lander E.S., Rogers J., RA Birney E., Hayashizaki Y.; RT "Analysis of the mouse transcriptome based on functional annotation of RT 60,770 full-length cDNAs."; RL Nature 420:563-573(2002). RN [4] RP SEQUENCE FROM N.A. RC STRAIN=Czech II; TISSUE=Breast tumor; RX MEDLINE=22388257; PubMed=12477932; DOI=10.1073/pnas.242603899; RA Strausberg R.L., Feingold E.A., Grouse L.H., Derge J.G., RA Klausner R.D., Collins F.S., Wagner L., Shenmen C.M., Schuler G.D., RA Altschul S.F., Zeeberg B., Buetow K.H., Schaefer C.F., Bhat N.K., RA Hopkins R.F., Jordan H., Moore T., Max S.I., Wang J., Hsieh F., RA Diatchenko L., Marusina K., Farmer A.A., Rubin G.M., Hong L., RA Stapleton M., Soares M.B., Bonaldo M.F., Casavant T.L., Scheetz T.E., RA Brownstein M.J., Usdin T.B., Toshiyuki S., Carninci P., Prange C., RA Raha S.S., Loquellano N.A., Peters G.J., Abramson R.D., Mullahy S.J., RA Bosak S.A., McEwan P.J., McKernan K.J., Malek J.A., Gunaratne P.H., RA Richards S., Worley K.C., Hale S., Garcia A.M., Gay L.J., Hulyk S.W., RA Villalon D.K., Muzny D.M., Sodergren E.J., Lu X., Gibbs R.A., RA Fahey J., Helton E., Ketteman M., Madan A., Rodrigues S., Sanchez A., RA Whiting M., Madan A., Young A.C., Shevchenko Y., Bouffard G.G., RA Blakesley R.W., Touchman J.W., Green E.D., Dickson M.C., RA Rodriguez A.C., Grimwood J., Schmutz J., Myers R.M., RA Butterfield Y.S.N., Krzywinski M.I., Skalska U., Smailus D.E., RA Schnerch A., Schein J.E., Jones S.J.M., Marra M.A.; RT "Generation and initial analysis of more than 15,000 full-length human RT and mouse cDNA sequences."; RL Proc. Natl. Acad. Sci. U.S.A. 99:16899-16903(2002). RN [5] RP SEQUENCE OF 1-94 FROM N.A. RX MEDLINE=86176739; PubMed=3960725; 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 [6] RP SEQUENCE OF 1-108 FROM N.A. RX MEDLINE=88122115; 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 [7] RP ETHANOLAMINE BINDING SITES, AND SEQUENCE OF 291-313 AND 372-376. RX MEDLINE=89340549; 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). CC -!- FUNCTION: This protein promotes the GTP-dependent binding of CC aminoacyl-tRNA to the A-site of ribosomes during protein CC biosynthesis. CC -!- SUBCELLULAR LOCATION: Cytoplasmic. CC -!- SIMILARITY: Belongs to the GTP-binding elongation factor family. CC EF-Tu/EF-1A subfamily. 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; -. DR EMBL; X13661; CAA31957.1; -. DR EMBL; AK032914; BAC28085.1; -. DR EMBL; AK076696; BAC36446.1; -. DR EMBL; AK081725; BAC38311.1; -. DR EMBL; AK083361; BAC38884.1; -. DR EMBL; BC004005; AAH04005.1; -. DR EMBL; BC004067; AAH04067.1; -. DR EMBL; BC005660; AAH05660.1; -. DR EMBL; BC018223; AAH18223.1; -. DR EMBL; BC018485; AAH18485.1; -. DR EMBL; X03688; CAA27324.1; -. DR EMBL; M17878; AAA37538.1; -. DR PIR; S02114; EFMS1. DR HSSP; P02994; 1F60. DR SWISS-2DPAGE; P10126; MOUSE. DR MGD; MGI:1096881; Eef1a1. DR InterPro; IPR004539; EF1_alpha. DR InterPro; IPR004160; EFTU_Cterm. DR InterPro; IPR004161; EFTU_D2. DR InterPro; IPR009001; Elong_init_C. DR InterPro; IPR000795; ProtSyn_GTPbind. DR InterPro; IPR009000; Translat_factor. 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 TIGRFAMs; TIGR00483; EF-1_alpha; 1. DR PROSITE; PS00301; EFACTOR_GTP; 1. KW Direct protein sequencing; Elongation factor; GTP-binding; KW Methylation; Multigene family; Protein biosynthesis. FT NP_BIND 14 21 GTP (By similarity). FT NP_BIND 91 95 GTP (By similarity). FT NP_BIND 153 156 GTP (By similarity). FT MOD_RES 36 36 N6,N6,N6-trimethyllysine (By similarity). FT MOD_RES 55 55 N6,N6-dimethyllysine (By similarity). FT MOD_RES 79 79 N6,N6,N6-trimethyllysine (By similarity). FT MOD_RES 165 165 N6,N6-dimethyllysine (By similarity). FT MOD_RES 318 318 N6,N6,N6-trimethyllysine (By similarity). FT BINDING 301 301 Ethanolamine-phosphoglycerol. FT BINDING 374 374 Ethanolamine-phosphoglycerol. FT CONFLICT 7 7 H -> R (in Ref. 6). FT CONFLICT 15 15 H -> L (in Ref. 6). FT CONFLICT 23 23 T -> S (in Ref. 6). FT CONFLICT 77 78 LW -> QR (in Ref. 2). FT CONFLICT 83 83 S -> A (in Ref. 5). FT CONFLICT 91 92 DA -> ES (in Ref. 2). FT CONFLICT 108 108 Q -> R (in Ref. 6). FT CONFLICT 156 156 D -> G (in Ref. 3; BAC28085). FT CONFLICT 222 222 S -> H (in Ref. 1). FT CONFLICT 224 226 SGT -> VAP (in Ref. 2). FT CONFLICT 225 225 G -> D (in Ref. 4; AAH04005). FT CONFLICT 239 239 Missing (in Ref. 2). FT CONFLICT 350 350 P -> T (in Ref. 3; BAC36446). 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 //