GenomeNet

Database: UniProt
Entry: P10126
LinkDB: P10126
Original site: P10126 
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   16-APR-2014, entry version 153.
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).
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 IFIT1 (via TPR repeats 4-7).
CC   -!- INTERACTION:
CC       Q01534:TSPY1 (xeno); NbExp=5; IntAct=EBI-773865, EBI-1973142;
CC   -!- SUBCELLULAR LOCATION: Cytoplasm. Nucleus (By similarity).
CC       Note=Colocalizes with DLC1 at actin-rich regions in the cell
CC       periphery (By similarity).
CC   -!- PTM: ISGylated.
CC   -!- PTM: Phosphorylated by TXK. Phosphorylation by PASK increases
CC       translation efficiency (By similarity).
CC   -!- SIMILARITY: Belongs to the GTP-binding elongation factor family.
CC       EF-Tu/EF-1A subfamily.
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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   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; 2-443.
DR   BioGrid; 199385; 12.
DR   DIP; DIP-46609N; -.
DR   IntAct; P10126; 25.
DR   MINT; MINT-1862449; -.
DR   PhosphoSite; P10126; -.
DR   SWISS-2DPAGE; P10126; -.
DR   PaxDb; P10126; -.
DR   PRIDE; P10126; -.
DR   Ensembl; ENSMUST00000042235; ENSMUSP00000042457; ENSMUSG00000037742.
DR   GeneID; 13627; -.
DR   KEGG; mmu:101056619; -.
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   NextBio; 284304; -.
DR   PRO; PR:P10126; -.
DR   Bgee; P10126; -.
DR   Genevestigator; P10126; -.
DR   GO; GO:0005737; C:cytoplasm; IDA:UniProtKB.
DR   GO; GO:0005634; C:nucleus; IEA:UniProtKB-SubCell.
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:0003746; F:translation elongation factor activity; IEA:UniProtKB-KW.
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; EFACTOR_GTP; 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   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; alternate (By
FT                                similarity).
FT   MOD_RES     165    165       N6-acetyllysine; alternate.
FT   MOD_RES     172    172       N6-acetyllysine.
FT   MOD_RES     273    273       N6-acetyllysine.
FT   MOD_RES     300    300       Phosphoserine; by TGFBR1 (By similarity).
FT   MOD_RES     301    301       5-glutamyl
FT                                glycerylphosphorylethanolamine.
FT   MOD_RES     318    318       N6,N6,N6-trimethyllysine (By similarity).
FT   MOD_RES     374    374       5-glutamyl
FT                                glycerylphosphorylethanolamine.
FT   MOD_RES     392    392       N6-acetyllysine; alternate.
FT   MOD_RES     392    392       N6-succinyllysine; alternate.
FT   MOD_RES     432    432       Phosphothreonine; by PASK (By
FT                                similarity).
FT   MOD_RES     439    439       N6-acetyllysine.
FT   CONFLICT      7      7       H -> R (in Ref. 5; AAA37538).
FT   CONFLICT     15     15       H -> L (in Ref. 5; AAA37538).
FT   CONFLICT     23     23       T -> S (in Ref. 5; AAA37538).
FT   CONFLICT     77     78       LW -> QR (in Ref. 2; CAA31957).
FT   CONFLICT     83     83       S -> A (in Ref. 6; CAA27324).
FT   CONFLICT     91     92       DA -> ES (in Ref. 2; CAA31957).
FT   CONFLICT    108    108       Q -> R (in Ref. 5; AAA37538).
FT   CONFLICT    156    156       D -> G (in Ref. 3; BAC28085).
FT   CONFLICT    222    222       S -> H (in Ref. 1; AAA50406).
FT   CONFLICT    224    226       SGT -> VAP (in Ref. 2; CAA31957).
FT   CONFLICT    225    225       G -> D (in Ref. 4; AAH04005).
FT   CONFLICT    239    239       Missing (in Ref. 2; CAA31957).
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
//
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