ID EF11_MOUSE STANDARD; PRT; 462 AA. AC P10126; DT 01-MAR-1989 (REL. 10, CREATED) DT 01-NOV-1995 (REL. 32, LAST SEQUENCE UPDATE) DT 01-NOV-1997 (REL. 35, LAST ANNOTATION UPDATE) DE ELONGATION FACTOR 1-ALPHA 1 (EF-1-ALPHA-1) (ELONGATION FACTOR TU) (EF- DE TU). GN EEF1A1 OR EEF1A. OS MUS MUSCULUS (MOUSE). OC EUKARYOTA; METAZOA; CHORDATA; VERTEBRATA; TETRAPODA; MAMMALIA; OC EUTHERIA; RODENTIA. RN [1] RP SEQUENCE FROM N.A. RX MEDLINE; 89108007. RA REDDY N.S., ROTH W.W., BRAGG P.W., WAHBA A.J.; RL GENE 70:231-243(1988). RN [2] RP SEQUENCE FROM N.A. RX MEDLINE; 89098401. RA LU X., WERNER D.; RL NUCLEIC ACIDS RES. 17:442-442(1989). RN [3] RP SEQUENCE OF 1-94 FROM N.A. RX MEDLINE; 86176739. RA RAO T.R., SLOBIN L.I.; RL NUCLEIC ACIDS RES. 14:2409-2409(1986). RN [4] RP ETHANOLAMINE BINDING SITES, AND SEQUENCE OF 291-313 AND 372-376. RX MEDLINE; 89340549. RA WHITEHEART S.W., SHENBAGARMURTHI P., CHEN L., COTTER R.J., RA HART G.W.; 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 --------------------------------------------------------------------------- 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; G556301; -. DR EMBL; X13661; G50797; -. DR EMBL; X03688; G50799; -. DR PIR; S02114; EFMS1. DR HSSP; P02990; 1ETU. DR MGD; MGI:95287; EEF1A. DR PROSITE; PS00301; EFACTOR_GTP; 1. KW ELONGATION FACTOR; PROTEIN BIOSYNTHESIS; GTP-BINDING; METHYLATION; KW MULTIGENE FAMILY. 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 METHYLATION (TRI-) (BY SIMILARITY). FT MOD_RES 55 55 METHYLATION (DI-) (BY SIMILARITY). FT MOD_RES 79 79 METHYLATION (TRI-) (BY SIMILARITY). FT MOD_RES 165 165 METHYLATION (DI-) (BY SIMILARITY). FT MOD_RES 318 318 METHYLATION (TRI-) (BY SIMILARITY). FT BINDING 301 301 ETHANOLAMINE-PHOSPHOGLYCEROL. FT BINDING 374 374 ETHANOLAMINE-PHOSPHOGLYCEROL. FT CONFLICT 77 78 LW -> QR (IN REF. 2). FT CONFLICT 83 83 S -> A (IN REF. 3). FT CONFLICT 91 92 DA -> ES (IN REF. 2). FT CONFLICT 222 226 HASGT -> SAVAP (IN REF. 2). FT CONFLICT 239 239 MISSING (IN REF. 2). SQ SEQUENCE 462 AA; 50164 MW; EE1A9CE1 CRC32; MGKEKTHINI VVIGHVDSGK STTTGHLIYK CGGIDKRTIE KFEKEAAEMG KGSFKYAWVL DKLKAERERG ITIDISLWKF ETSKYYVTII DAPGHRDFIK NMITGTSQAD CAVLIVAAGV GEFEAGISKN GQTREHALLA YTLGVKQLIV GVNKMDSTEP PYSQKRYEEI VKEVSTYIKK IGYNPDTVAF VPISGWNGDN MLEPSANMPW FKGWKVTRKD GHASGTTLLE ALDCILPPTR PTDKPLRLPL QDVYKIGGIG TVPVGRVETG VLKPGMVVTF APVNVTTEVK SVEMHHEALS EALPGDNVGF NVKNVSVKDV RRGNVAGDSK NDPPMEAAGF TAQVIILNHP GQISAGYAPV LDCHTAHIAC KFAELKEKID RRSGKKLEDG PKFLKSGDAA IVDMVPGKPM CVESFSDYPP LGRFAVRDMR QTVAVGVIKA VDKKAAGAGK VTKSAQKAQK AK //