Full text data of EEF1A1
EEF1A1
(EEF1A, EF1A, LENG7)
[Confidence: high (present in two of the MS resources)]
Elongation factor 1-alpha 1; EF-1-alpha-1 (Elongation factor Tu; EF-Tu; Eukaryotic elongation factor 1 A-1; eEF1A-1; Leukocyte receptor cluster member 7)
Note: presumably soluble (membrane word is not in UniProt keywords or features)
Elongation factor 1-alpha 1; EF-1-alpha-1 (Elongation factor Tu; EF-Tu; Eukaryotic elongation factor 1 A-1; eEF1A-1; Leukocyte receptor cluster member 7)
Note: presumably soluble (membrane word is not in UniProt keywords or features)
hRBCD
IPI00025447
IPI00025447 Elongation factor 1-alpha 1 bone marrow, B cell, lymph, This protein promotes the GTP-dependent binding of aminoacyl-tRNA to the A-site of ribosomes during protein biosynthesis. soluble n/a n/a n/a n/a n/a n/a n/a n/a n/a n/a n/a n/a n/a n/a n/a n/a n/a n/a n/a n/a cytoplasmic n/a found at its expected molecular weight found at molecular weight
IPI00025447 Elongation factor 1-alpha 1 bone marrow, B cell, lymph, This protein promotes the GTP-dependent binding of aminoacyl-tRNA to the A-site of ribosomes during protein biosynthesis. soluble n/a n/a n/a n/a n/a n/a n/a n/a n/a n/a n/a n/a n/a n/a n/a n/a n/a n/a n/a n/a cytoplasmic n/a found at its expected molecular weight found at molecular weight
UniProt
P68104
ID EF1A1_HUMAN Reviewed; 462 AA.
AC P68104; P04719; P04720;
DT 13-AUG-1987, integrated into UniProtKB/Swiss-Prot.
read moreDT 13-AUG-1987, sequence version 1.
DT 22-JAN-2014, entry version 123.
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;
DE AltName: Full=Leukocyte receptor cluster member 7;
GN Name=EEF1A1; Synonyms=EEF1A, EF1A, LENG7;
OS Homo sapiens (Human).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
OC Catarrhini; Hominidae; Homo.
OX NCBI_TaxID=9606;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA].
RX PubMed=3512269; DOI=10.1111/j.1432-1033.1986.tb09472.x;
RA Brands J.H.G.M., Maassen J.A., van Hemert F.J., Amons R., Moeller W.;
RT "The primary structure of the alpha subunit of human elongation factor
RT 1. Structural aspects of guanine-nucleotide-binding sites.";
RL Eur. J. Biochem. 155:167-171(1986).
RN [2]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RX PubMed=2564392;
RA Uetsuki T., Naito A., Nagata S., Kaziro Y.;
RT "Isolation and characterization of the human chromosomal gene for
RT polypeptide chain elongation factor-1 alpha.";
RL J. Biol. Chem. 264:5791-5798(1989).
RN [3]
RP NUCLEOTIDE SEQUENCE [MRNA].
RC TISSUE=Liver;
RX PubMed=2183196; DOI=10.1093/nar/18.6.1513;
RA Madsen H.O., Poulsen K., Dahl O., Clark B.F.C., Hjorth J.P.;
RT "Retropseudogenes constitute the major part of the human elongation
RT factor 1 alpha gene family.";
RL Nucleic Acids Res. 18:1513-1516(1990).
RN [4]
RP NUCLEOTIDE SEQUENCE [MRNA].
RA Shimazu T., Koike K.;
RT "Postnatal expression of a novel mRNA isoform from the human
RT elongation factor-1a gene.";
RL Submitted (JUL-2001) to the EMBL/GenBank/DDBJ databases.
RN [5]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC TISSUE=B-cell, Bone marrow, Cervix, Colon, Hippocampus, Lung, Lymph,
RC Mammary gland, Ovary, Pancreas, Placenta, Testis, and Uterus;
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 [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; 52-62; 85-96; 101-129; 135-180; 248-313;
RP 396-423 AND 431-439, METHYLATION AT LYS-55 AND LYS-165, AND MASS
RP SPECTROMETRY.
RC TISSUE=Colon carcinoma, and Ovarian carcinoma;
RA Bienvenut W.V., Zebisch A., Kolch W.;
RL Submitted (JAN-2010) to UniProtKB.
RN [8]
RP PROTEIN SEQUENCE OF 7-16 AND 85-96, INTERACTION WITH PARP1 AND TXK,
RP PHOSPHORYLATION BY TXK, SUBCELLULAR LOCATION, AND FUNCTION AS A
RP TRANSCRIPTION FACTOR.
RX PubMed=17177976; DOI=10.1111/j.1365-2249.2006.03249.x;
RA Maruyama T., Nara K., Yoshikawa H., Suzuki N.;
RT "Txk, a member of the non-receptor tyrosine kinase of the Tec family,
RT forms a complex with poly(ADP-ribose) polymerase 1 and elongation
RT factor 1alpha and regulates interferon-gamma gene transcription in Th1
RT cells.";
RL Clin. Exp. Immunol. 147:164-175(2007).
RN [9]
RP PROTEIN SEQUENCE OF 38-44; 70-79; 85-96; 135-172; 248-290; 386-392 AND
RP 428-439.
RC TISSUE=B-cell lymphoma;
RA Bienvenut W.V.;
RL Submitted (JUN-2005) to UniProtKB.
RN [10]
RP NUCLEOTIDE SEQUENCE [MRNA] OF 138-462.
RX PubMed=3346208;
RA Ann D.K., Wu M.M.J., Huang T., Carlson D.M., Wu R.;
RT "Retinol-regulated gene expression in human tracheobronchial
RT epithelial cells. Enhanced expression of elongation factor EF-1
RT alpha.";
RL J. Biol. Chem. 263:3546-3549(1988).
RN [11]
RP ETHANOLAMINYLATION AT 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 [12]
RP INDUCTION BY HOMOCYSTEINE.
RX PubMed=9677419; DOI=10.1074/jbc.273.31.19840;
RA Chacko G., Ling Q., Hajjar K.A.;
RT "Induction of acute translational response genes by homocysteine.
RT Elongation factors-1alpha, -beta, and -delta.";
RL J. Biol. Chem. 273:19840-19846(1998).
RN [13]
RP IDENTIFICATION IN A NUCLEAR EXPORT RECEPTOR COMPLEX WITH XPO5; RAN AND
RP TRNA, AND INTERACTION WITH XPO5.
RX PubMed=12426392; DOI=10.1093/emboj/cdf613;
RA Bohnsack M.T., Regener K., Schwappach B., Saffrich R., Paraskeva E.,
RA Hartmann E., Goerlich D.;
RT "Exp5 exports eEF1A via tRNA from nuclei and synergizes with other
RT transport pathways to confine translation to the cytoplasm.";
RL EMBO J. 21:6205-6215(2002).
RN [14]
RP IDENTIFICATION IN A NUCLEAR EXPORT RECEPTOR COMPLEX WITH XPO5; RAN AND
RP TRNA, AND INTERACTION WITH XPO5.
RX PubMed=12426393; DOI=10.1093/emboj/cdf620;
RA Calado A., Treichel N., Mueller E.-C., Otto A., Kutay U.;
RT "Exportin-5-mediated nuclear export of eukaryotic elongation factor 1A
RT and tRNA.";
RL EMBO J. 21:6216-6224(2002).
RN [15]
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 [16]
RP PHOSPHORYLATION AT THR-432, AND MUTAGENESIS OF THR-432.
RX PubMed=17595531; DOI=10.1159/000104169;
RA Eckhardt K., Troger J., Reissmann J., Katschinski D.M., Wagner K.F.,
RA Stengel P., Paasch U., Hunziker P., Borter E., Barth S., Schlafli P.,
RA Spielmann P., Stiehl D.P., Camenisch G., Wenger R.H.;
RT "Male germ cell expression of the PAS domain kinase PASKIN and its
RT novel target eukaryotic translation elongation factor eEF1A1.";
RL Cell. Physiol. Biochem. 20:227-240(2007).
RN [17]
RP INTERACTION WITH KARS.
RX PubMed=18029264; DOI=10.1016/j.bbrc.2007.11.028;
RA Guzzo C.M., Yang D.C.H.;
RT "Lysyl-tRNA synthetase interacts with EF1alpha, aspartyl-tRNA
RT synthetase and p38 in vitro.";
RL Biochem. Biophys. Res. Commun. 365:718-723(2008).
RN [18]
RP INTERACTION WITH ERGIC2.
RX PubMed=17980171; DOI=10.1016/j.bbapap.2007.10.006;
RA Yang Y.F., Chou M.Y., Fan C.Y., Chen S.F., Lyu P.C., Liu C.C.,
RA Tseng T.L.;
RT "The possible interaction of CDA14 and protein elongation factor
RT 1alpha.";
RL Biochim. Biophys. Acta 1784:312-318(2008).
RN [19]
RP INTERACTION WITH DLC1, AND SUBCELLULAR LOCATION.
RX PubMed=19158340; DOI=10.1242/jcs.027482;
RA Zhong D., Zhang J., Yang S., Soh U.J., Buschdorf J.P., Zhou Y.T.,
RA Yang D., Low B.C.;
RT "The SAM domain of the RhoGAP DLC1 binds EF1A1 to regulate cell
RT migration.";
RL J. Cell Sci. 122:414-424(2009).
RN [20]
RP PHOSPHORYLATION AT SER-300.
RX PubMed=20832312; DOI=10.1016/j.cub.2010.08.017;
RA Lin K.W., Yakymovych I., Jia M., Yakymovych M., Souchelnytskyi S.;
RT "Phosphorylation of eEF1A1 at Ser300 by TbetaR-I results in inhibition
RT of mRNA translation.";
RL Curr. Biol. 20:1615-1625(2010).
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.
CC -!- SUBUNIT: Found in a nuclear export complex with XPO5, EEF1A1, Ran
CC and aminoacylated tRNA. Interacts with PARP1, TXK, XPO5 and KARS.
CC May interact with ERGIC2. Interacts with IFIT1 (via TPR repeats 4-
CC 7) (By similarity). Interacts with DLC1, facilitating distribution
CC to the membrane periphery and ruffles upon growth factor
CC stimulation.
CC -!- INTERACTION:
CC Q8NFJ9:BBS1; NbExp=3; IntAct=EBI-352162, EBI-1805484;
CC Q00987:MDM2; NbExp=9; IntAct=EBI-352162, EBI-389668;
CC P54725:RAD23A; NbExp=2; IntAct=EBI-352162, EBI-746453;
CC Q9NYA1:SPHK1; NbExp=2; IntAct=EBI-352162, EBI-985303;
CC P63104:YWHAZ; NbExp=2; IntAct=EBI-352162, EBI-347088;
CC Q05516:ZBTB16; NbExp=4; IntAct=EBI-352162, EBI-711925;
CC -!- SUBCELLULAR LOCATION: Cytoplasm. Nucleus. Note=Colocalizes with
CC DLC1 at actin-rich regions in the cell periphery.
CC -!- TISSUE SPECIFICITY: Brain, placenta, lung, liver, kidney, pancreas
CC but barely detectable in heart and skeletal muscle.
CC -!- INDUCTION: By homocysteine (HC), may mediate accelerated synthesis
CC of free thiol-containing proteins in response to HC-induced
CC oxidative stress.
CC -!- PTM: ISGylated.
CC -!- PTM: Phosphorylated by TXK. Phosphorylation by PASK increases
CC translation efficiency.
CC -!- SIMILARITY: Belongs to the GTP-binding elongation factor family.
CC EF-Tu/EF-1A subfamily.
CC -!- SEQUENCE CAUTION:
CC Sequence=AAA52367.1; Type=Erroneous initiation;
CC -!- WEB RESOURCE: Name=Atlas of Genetics and Cytogenetics in Oncology
CC and Haematology;
CC URL="http://atlasgeneticsoncology.org/Genes/EEF1A1ID40407ch6q13.html";
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DR EMBL; X03558; CAA27245.1; -; mRNA.
DR EMBL; J04617; AAA52343.1; -; Genomic_DNA.
DR EMBL; X16869; CAA34756.1; -; mRNA.
DR EMBL; AY043301; AAK95378.1; -; mRNA.
DR EMBL; BC008587; AAH08587.1; -; mRNA.
DR EMBL; BC009733; AAH09733.1; -; mRNA.
DR EMBL; BC009875; AAH09875.1; -; mRNA.
DR EMBL; BC010735; AAH10735.1; -; mRNA.
DR EMBL; BC012891; AAH12891.1; -; mRNA.
DR EMBL; BC014224; AAH14224.1; -; mRNA.
DR EMBL; BC018150; AAH18150.1; -; mRNA.
DR EMBL; BC018641; AAH18641.1; -; mRNA.
DR EMBL; BC021686; AAH21686.1; -; mRNA.
DR EMBL; BC028674; AAH28674.1; -; mRNA.
DR EMBL; BC038339; AAH38339.1; -; mRNA.
DR EMBL; BC057391; AAH57391.1; -; mRNA.
DR EMBL; BC066893; AAH66893.1; -; mRNA.
DR EMBL; BC072385; AAH72385.1; -; mRNA.
DR EMBL; BC082268; AAH82268.1; -; mRNA.
DR EMBL; X03689; CAA27325.1; -; mRNA.
DR EMBL; M29548; AAA52367.1; ALT_INIT; mRNA.
DR PIR; B24977; EFHU1.
DR RefSeq; NP_001393.1; NM_001402.5.
DR RefSeq; XP_005248723.1; XM_005248666.1.
DR RefSeq; XP_005248724.1; XM_005248667.1.
DR UniGene; Hs.535192; -.
DR UniGene; Hs.586423; -.
DR UniGene; Hs.745122; -.
DR PDB; 1SYW; Model; -; A=2-443.
DR PDBsum; 1SYW; -.
DR ProteinModelPortal; P68104; -.
DR SMR; P68104; 2-443.
DR IntAct; P68104; 162.
DR MINT; MINT-1180846; -.
DR STRING; 9606.ENSP00000330054; -.
DR BindingDB; P68104; -.
DR ChEMBL; CHEMBL1795120; -.
DR PhosphoSite; P68104; -.
DR DMDM; 55584035; -.
DR OGP; P68104; -.
DR SWISS-2DPAGE; P68104; -.
DR UCD-2DPAGE; P68104; -.
DR PaxDb; P68104; -.
DR PRIDE; P68104; -.
DR DNASU; 1915; -.
DR Ensembl; ENST00000309268; ENSP00000339053; ENSG00000156508.
DR Ensembl; ENST00000316292; ENSP00000339063; ENSG00000156508.
DR Ensembl; ENST00000331523; ENSP00000330054; ENSG00000156508.
DR GeneID; 1915; -.
DR KEGG; hsa:1915; -.
DR UCSC; uc003phi.3; human.
DR CTD; 1915; -.
DR GeneCards; GC06M074225; -.
DR H-InvDB; HIX0020005; -.
DR H-InvDB; HIX0032108; -.
DR H-InvDB; HIX0033669; -.
DR H-InvDB; HIX0169110; -.
DR HGNC; HGNC:3189; EEF1A1.
DR MIM; 130590; gene.
DR neXtProt; NX_P68104; -.
DR PharmGKB; PA27625; -.
DR eggNOG; COG5256; -.
DR HOGENOM; HOG000229291; -.
DR HOVERGEN; HBG000179; -.
DR InParanoid; P68104; -.
DR KO; K03231; -.
DR OMA; AIRDMGM; -.
DR OrthoDB; EOG7NKKK3; -.
DR PhylomeDB; P68104; -.
DR Reactome; REACT_17015; Metabolism of proteins.
DR Reactome; REACT_71; Gene Expression.
DR SignaLink; P68104; -.
DR ChiTaRS; EEF1A1; human.
DR GeneWiki; Eukaryotic_translation_elongation_factor_1_alpha_1; -.
DR GenomeRNAi; 1915; -.
DR NextBio; 7799; -.
DR PMAP-CutDB; P68104; -.
DR PRO; PR:P68104; -.
DR ArrayExpress; P68104; -.
DR Bgee; P68104; -.
DR CleanEx; HS_EEF1A1; -.
DR Genevestigator; P68104; -.
DR GO; GO:0005829; C:cytosol; TAS:Reactome.
DR GO; GO:0005853; C:eukaryotic translation elongation factor 1 complex; TAS:UniProtKB.
DR GO; GO:0005634; C:nucleus; IEA:UniProtKB-SubCell.
DR GO; GO:0005886; C:plasma membrane; IEA:Ensembl.
DR GO; GO:0005525; F:GTP binding; TAS:UniProtKB.
DR GO; GO:0003924; F:GTPase activity; IEA:InterPro.
DR GO; GO:0003746; F:translation elongation factor activity; TAS:UniProtKB.
DR GO; GO:0006184; P:GTP catabolic process; IEA:GOC.
DR GO; GO:0006355; P:regulation of transcription, DNA-dependent; IEA:UniProtKB-KW.
DR GO; GO:0006351; P:transcription, DNA-dependent; IEA:UniProtKB-KW.
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 3D-structure; Complete proteome; Cytoplasm; Direct protein sequencing;
KW Elongation factor; GTP-binding; Methylation; Nucleotide-binding;
KW Nucleus; Phosphoprotein; Protein biosynthesis; Reference proteome;
KW Transcription; Transcription regulation; Ubl conjugation.
FT CHAIN 1 462 Elongation factor 1-alpha 1.
FT /FTId=PRO_0000090885.
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.
FT MOD_RES 79 79 N6,N6,N6-trimethyllysine (By similarity).
FT MOD_RES 165 165 N6,N6-dimethyllysine.
FT MOD_RES 300 300 Phosphoserine; by TGFBR1.
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 432 432 Phosphothreonine; by PASK.
FT MUTAGEN 432 432 T->A: Abolishes phosphorylation by PASK.
FT CONFLICT 83 83 S -> A (in Ref. 6; CAA27325).
FT CONFLICT 232 232 L -> V (in Ref. 3; CAA34756).
FT STRAND 7 14
FT HELIX 20 31
FT TURN 34 36
FT HELIX 37 46
FT TURN 47 49
FT HELIX 51 53
FT HELIX 56 60
FT HELIX 61 63
FT TURN 64 66
FT STRAND 76 81
FT STRAND 86 91
FT HELIX 96 101
FT HELIX 103 106
FT STRAND 110 116
FT HELIX 124 127
FT HELIX 132 134
FT HELIX 136 143
FT STRAND 148 152
FT TURN 160 162
FT HELIX 164 166
FT HELIX 168 178
FT TURN 179 181
FT HELIX 185 187
FT STRAND 188 192
FT TURN 195 198
FT STRAND 199 203
FT STRAND 214 218
FT STRAND 221 227
FT HELIX 228 232
FT STRAND 243 245
FT STRAND 247 256
FT TURN 257 259
FT STRAND 260 265
FT STRAND 277 283
FT STRAND 286 293
FT STRAND 300 302
FT STRAND 309 314
FT TURN 317 319
FT STRAND 325 328
FT TURN 329 331
FT STRAND 337 346
FT STRAND 352 354
FT STRAND 360 363
FT STRAND 366 380
FT TURN 381 383
FT STRAND 392 395
FT STRAND 398 408
FT TURN 415 417
FT HELIX 419 422
FT STRAND 423 428
FT STRAND 431 442
SQ SEQUENCE 462 AA; 50141 MW; D465615545AF686A CRC64;
MGKEKTHINI VVIGHVDSGK STTTGHLIYK CGGIDKRTIE KFEKEAAEMG KGSFKYAWVL
DKLKAERERG ITIDISLWKF ETSKYYVTII DAPGHRDFIK NMITGTSQAD CAVLIVAAGV
GEFEAGISKN GQTREHALLA YTLGVKQLIV GVNKMDSTEP PYSQKRYEEI VKEVSTYIKK
IGYNPDTVAF VPISGWNGDN MLEPSANMPW FKGWKVTRKD GNASGTTLLE ALDCILPPTR
PTDKPLRLPL QDVYKIGGIG TVPVGRVETG VLKPGMVVTF APVNVTTEVK SVEMHHEALS
EALPGDNVGF NVKNVSVKDV RRGNVAGDSK NDPPMEAAGF TAQVIILNHP GQISAGYAPV
LDCHTAHIAC KFAELKEKID RRSGKKLEDG PKFLKSGDAA IVDMVPGKPM CVESFSDYPP
LGRFAVRDMR QTVAVGVIKA VDKKAAGAGK VTKSAQKAQK AK
//
ID EF1A1_HUMAN Reviewed; 462 AA.
AC P68104; P04719; P04720;
DT 13-AUG-1987, integrated into UniProtKB/Swiss-Prot.
read moreDT 13-AUG-1987, sequence version 1.
DT 22-JAN-2014, entry version 123.
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;
DE AltName: Full=Leukocyte receptor cluster member 7;
GN Name=EEF1A1; Synonyms=EEF1A, EF1A, LENG7;
OS Homo sapiens (Human).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
OC Catarrhini; Hominidae; Homo.
OX NCBI_TaxID=9606;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA].
RX PubMed=3512269; DOI=10.1111/j.1432-1033.1986.tb09472.x;
RA Brands J.H.G.M., Maassen J.A., van Hemert F.J., Amons R., Moeller W.;
RT "The primary structure of the alpha subunit of human elongation factor
RT 1. Structural aspects of guanine-nucleotide-binding sites.";
RL Eur. J. Biochem. 155:167-171(1986).
RN [2]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RX PubMed=2564392;
RA Uetsuki T., Naito A., Nagata S., Kaziro Y.;
RT "Isolation and characterization of the human chromosomal gene for
RT polypeptide chain elongation factor-1 alpha.";
RL J. Biol. Chem. 264:5791-5798(1989).
RN [3]
RP NUCLEOTIDE SEQUENCE [MRNA].
RC TISSUE=Liver;
RX PubMed=2183196; DOI=10.1093/nar/18.6.1513;
RA Madsen H.O., Poulsen K., Dahl O., Clark B.F.C., Hjorth J.P.;
RT "Retropseudogenes constitute the major part of the human elongation
RT factor 1 alpha gene family.";
RL Nucleic Acids Res. 18:1513-1516(1990).
RN [4]
RP NUCLEOTIDE SEQUENCE [MRNA].
RA Shimazu T., Koike K.;
RT "Postnatal expression of a novel mRNA isoform from the human
RT elongation factor-1a gene.";
RL Submitted (JUL-2001) to the EMBL/GenBank/DDBJ databases.
RN [5]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC TISSUE=B-cell, Bone marrow, Cervix, Colon, Hippocampus, Lung, Lymph,
RC Mammary gland, Ovary, Pancreas, Placenta, Testis, and Uterus;
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 [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; 52-62; 85-96; 101-129; 135-180; 248-313;
RP 396-423 AND 431-439, METHYLATION AT LYS-55 AND LYS-165, AND MASS
RP SPECTROMETRY.
RC TISSUE=Colon carcinoma, and Ovarian carcinoma;
RA Bienvenut W.V., Zebisch A., Kolch W.;
RL Submitted (JAN-2010) to UniProtKB.
RN [8]
RP PROTEIN SEQUENCE OF 7-16 AND 85-96, INTERACTION WITH PARP1 AND TXK,
RP PHOSPHORYLATION BY TXK, SUBCELLULAR LOCATION, AND FUNCTION AS A
RP TRANSCRIPTION FACTOR.
RX PubMed=17177976; DOI=10.1111/j.1365-2249.2006.03249.x;
RA Maruyama T., Nara K., Yoshikawa H., Suzuki N.;
RT "Txk, a member of the non-receptor tyrosine kinase of the Tec family,
RT forms a complex with poly(ADP-ribose) polymerase 1 and elongation
RT factor 1alpha and regulates interferon-gamma gene transcription in Th1
RT cells.";
RL Clin. Exp. Immunol. 147:164-175(2007).
RN [9]
RP PROTEIN SEQUENCE OF 38-44; 70-79; 85-96; 135-172; 248-290; 386-392 AND
RP 428-439.
RC TISSUE=B-cell lymphoma;
RA Bienvenut W.V.;
RL Submitted (JUN-2005) to UniProtKB.
RN [10]
RP NUCLEOTIDE SEQUENCE [MRNA] OF 138-462.
RX PubMed=3346208;
RA Ann D.K., Wu M.M.J., Huang T., Carlson D.M., Wu R.;
RT "Retinol-regulated gene expression in human tracheobronchial
RT epithelial cells. Enhanced expression of elongation factor EF-1
RT alpha.";
RL J. Biol. Chem. 263:3546-3549(1988).
RN [11]
RP ETHANOLAMINYLATION AT 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 [12]
RP INDUCTION BY HOMOCYSTEINE.
RX PubMed=9677419; DOI=10.1074/jbc.273.31.19840;
RA Chacko G., Ling Q., Hajjar K.A.;
RT "Induction of acute translational response genes by homocysteine.
RT Elongation factors-1alpha, -beta, and -delta.";
RL J. Biol. Chem. 273:19840-19846(1998).
RN [13]
RP IDENTIFICATION IN A NUCLEAR EXPORT RECEPTOR COMPLEX WITH XPO5; RAN AND
RP TRNA, AND INTERACTION WITH XPO5.
RX PubMed=12426392; DOI=10.1093/emboj/cdf613;
RA Bohnsack M.T., Regener K., Schwappach B., Saffrich R., Paraskeva E.,
RA Hartmann E., Goerlich D.;
RT "Exp5 exports eEF1A via tRNA from nuclei and synergizes with other
RT transport pathways to confine translation to the cytoplasm.";
RL EMBO J. 21:6205-6215(2002).
RN [14]
RP IDENTIFICATION IN A NUCLEAR EXPORT RECEPTOR COMPLEX WITH XPO5; RAN AND
RP TRNA, AND INTERACTION WITH XPO5.
RX PubMed=12426393; DOI=10.1093/emboj/cdf620;
RA Calado A., Treichel N., Mueller E.-C., Otto A., Kutay U.;
RT "Exportin-5-mediated nuclear export of eukaryotic elongation factor 1A
RT and tRNA.";
RL EMBO J. 21:6216-6224(2002).
RN [15]
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 [16]
RP PHOSPHORYLATION AT THR-432, AND MUTAGENESIS OF THR-432.
RX PubMed=17595531; DOI=10.1159/000104169;
RA Eckhardt K., Troger J., Reissmann J., Katschinski D.M., Wagner K.F.,
RA Stengel P., Paasch U., Hunziker P., Borter E., Barth S., Schlafli P.,
RA Spielmann P., Stiehl D.P., Camenisch G., Wenger R.H.;
RT "Male germ cell expression of the PAS domain kinase PASKIN and its
RT novel target eukaryotic translation elongation factor eEF1A1.";
RL Cell. Physiol. Biochem. 20:227-240(2007).
RN [17]
RP INTERACTION WITH KARS.
RX PubMed=18029264; DOI=10.1016/j.bbrc.2007.11.028;
RA Guzzo C.M., Yang D.C.H.;
RT "Lysyl-tRNA synthetase interacts with EF1alpha, aspartyl-tRNA
RT synthetase and p38 in vitro.";
RL Biochem. Biophys. Res. Commun. 365:718-723(2008).
RN [18]
RP INTERACTION WITH ERGIC2.
RX PubMed=17980171; DOI=10.1016/j.bbapap.2007.10.006;
RA Yang Y.F., Chou M.Y., Fan C.Y., Chen S.F., Lyu P.C., Liu C.C.,
RA Tseng T.L.;
RT "The possible interaction of CDA14 and protein elongation factor
RT 1alpha.";
RL Biochim. Biophys. Acta 1784:312-318(2008).
RN [19]
RP INTERACTION WITH DLC1, AND SUBCELLULAR LOCATION.
RX PubMed=19158340; DOI=10.1242/jcs.027482;
RA Zhong D., Zhang J., Yang S., Soh U.J., Buschdorf J.P., Zhou Y.T.,
RA Yang D., Low B.C.;
RT "The SAM domain of the RhoGAP DLC1 binds EF1A1 to regulate cell
RT migration.";
RL J. Cell Sci. 122:414-424(2009).
RN [20]
RP PHOSPHORYLATION AT SER-300.
RX PubMed=20832312; DOI=10.1016/j.cub.2010.08.017;
RA Lin K.W., Yakymovych I., Jia M., Yakymovych M., Souchelnytskyi S.;
RT "Phosphorylation of eEF1A1 at Ser300 by TbetaR-I results in inhibition
RT of mRNA translation.";
RL Curr. Biol. 20:1615-1625(2010).
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.
CC -!- SUBUNIT: Found in a nuclear export complex with XPO5, EEF1A1, Ran
CC and aminoacylated tRNA. Interacts with PARP1, TXK, XPO5 and KARS.
CC May interact with ERGIC2. Interacts with IFIT1 (via TPR repeats 4-
CC 7) (By similarity). Interacts with DLC1, facilitating distribution
CC to the membrane periphery and ruffles upon growth factor
CC stimulation.
CC -!- INTERACTION:
CC Q8NFJ9:BBS1; NbExp=3; IntAct=EBI-352162, EBI-1805484;
CC Q00987:MDM2; NbExp=9; IntAct=EBI-352162, EBI-389668;
CC P54725:RAD23A; NbExp=2; IntAct=EBI-352162, EBI-746453;
CC Q9NYA1:SPHK1; NbExp=2; IntAct=EBI-352162, EBI-985303;
CC P63104:YWHAZ; NbExp=2; IntAct=EBI-352162, EBI-347088;
CC Q05516:ZBTB16; NbExp=4; IntAct=EBI-352162, EBI-711925;
CC -!- SUBCELLULAR LOCATION: Cytoplasm. Nucleus. Note=Colocalizes with
CC DLC1 at actin-rich regions in the cell periphery.
CC -!- TISSUE SPECIFICITY: Brain, placenta, lung, liver, kidney, pancreas
CC but barely detectable in heart and skeletal muscle.
CC -!- INDUCTION: By homocysteine (HC), may mediate accelerated synthesis
CC of free thiol-containing proteins in response to HC-induced
CC oxidative stress.
CC -!- PTM: ISGylated.
CC -!- PTM: Phosphorylated by TXK. Phosphorylation by PASK increases
CC translation efficiency.
CC -!- SIMILARITY: Belongs to the GTP-binding elongation factor family.
CC EF-Tu/EF-1A subfamily.
CC -!- SEQUENCE CAUTION:
CC Sequence=AAA52367.1; Type=Erroneous initiation;
CC -!- WEB RESOURCE: Name=Atlas of Genetics and Cytogenetics in Oncology
CC and Haematology;
CC URL="http://atlasgeneticsoncology.org/Genes/EEF1A1ID40407ch6q13.html";
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DR EMBL; X03558; CAA27245.1; -; mRNA.
DR EMBL; J04617; AAA52343.1; -; Genomic_DNA.
DR EMBL; X16869; CAA34756.1; -; mRNA.
DR EMBL; AY043301; AAK95378.1; -; mRNA.
DR EMBL; BC008587; AAH08587.1; -; mRNA.
DR EMBL; BC009733; AAH09733.1; -; mRNA.
DR EMBL; BC009875; AAH09875.1; -; mRNA.
DR EMBL; BC010735; AAH10735.1; -; mRNA.
DR EMBL; BC012891; AAH12891.1; -; mRNA.
DR EMBL; BC014224; AAH14224.1; -; mRNA.
DR EMBL; BC018150; AAH18150.1; -; mRNA.
DR EMBL; BC018641; AAH18641.1; -; mRNA.
DR EMBL; BC021686; AAH21686.1; -; mRNA.
DR EMBL; BC028674; AAH28674.1; -; mRNA.
DR EMBL; BC038339; AAH38339.1; -; mRNA.
DR EMBL; BC057391; AAH57391.1; -; mRNA.
DR EMBL; BC066893; AAH66893.1; -; mRNA.
DR EMBL; BC072385; AAH72385.1; -; mRNA.
DR EMBL; BC082268; AAH82268.1; -; mRNA.
DR EMBL; X03689; CAA27325.1; -; mRNA.
DR EMBL; M29548; AAA52367.1; ALT_INIT; mRNA.
DR PIR; B24977; EFHU1.
DR RefSeq; NP_001393.1; NM_001402.5.
DR RefSeq; XP_005248723.1; XM_005248666.1.
DR RefSeq; XP_005248724.1; XM_005248667.1.
DR UniGene; Hs.535192; -.
DR UniGene; Hs.586423; -.
DR UniGene; Hs.745122; -.
DR PDB; 1SYW; Model; -; A=2-443.
DR PDBsum; 1SYW; -.
DR ProteinModelPortal; P68104; -.
DR SMR; P68104; 2-443.
DR IntAct; P68104; 162.
DR MINT; MINT-1180846; -.
DR STRING; 9606.ENSP00000330054; -.
DR BindingDB; P68104; -.
DR ChEMBL; CHEMBL1795120; -.
DR PhosphoSite; P68104; -.
DR DMDM; 55584035; -.
DR OGP; P68104; -.
DR SWISS-2DPAGE; P68104; -.
DR UCD-2DPAGE; P68104; -.
DR PaxDb; P68104; -.
DR PRIDE; P68104; -.
DR DNASU; 1915; -.
DR Ensembl; ENST00000309268; ENSP00000339053; ENSG00000156508.
DR Ensembl; ENST00000316292; ENSP00000339063; ENSG00000156508.
DR Ensembl; ENST00000331523; ENSP00000330054; ENSG00000156508.
DR GeneID; 1915; -.
DR KEGG; hsa:1915; -.
DR UCSC; uc003phi.3; human.
DR CTD; 1915; -.
DR GeneCards; GC06M074225; -.
DR H-InvDB; HIX0020005; -.
DR H-InvDB; HIX0032108; -.
DR H-InvDB; HIX0033669; -.
DR H-InvDB; HIX0169110; -.
DR HGNC; HGNC:3189; EEF1A1.
DR MIM; 130590; gene.
DR neXtProt; NX_P68104; -.
DR PharmGKB; PA27625; -.
DR eggNOG; COG5256; -.
DR HOGENOM; HOG000229291; -.
DR HOVERGEN; HBG000179; -.
DR InParanoid; P68104; -.
DR KO; K03231; -.
DR OMA; AIRDMGM; -.
DR OrthoDB; EOG7NKKK3; -.
DR PhylomeDB; P68104; -.
DR Reactome; REACT_17015; Metabolism of proteins.
DR Reactome; REACT_71; Gene Expression.
DR SignaLink; P68104; -.
DR ChiTaRS; EEF1A1; human.
DR GeneWiki; Eukaryotic_translation_elongation_factor_1_alpha_1; -.
DR GenomeRNAi; 1915; -.
DR NextBio; 7799; -.
DR PMAP-CutDB; P68104; -.
DR PRO; PR:P68104; -.
DR ArrayExpress; P68104; -.
DR Bgee; P68104; -.
DR CleanEx; HS_EEF1A1; -.
DR Genevestigator; P68104; -.
DR GO; GO:0005829; C:cytosol; TAS:Reactome.
DR GO; GO:0005853; C:eukaryotic translation elongation factor 1 complex; TAS:UniProtKB.
DR GO; GO:0005634; C:nucleus; IEA:UniProtKB-SubCell.
DR GO; GO:0005886; C:plasma membrane; IEA:Ensembl.
DR GO; GO:0005525; F:GTP binding; TAS:UniProtKB.
DR GO; GO:0003924; F:GTPase activity; IEA:InterPro.
DR GO; GO:0003746; F:translation elongation factor activity; TAS:UniProtKB.
DR GO; GO:0006184; P:GTP catabolic process; IEA:GOC.
DR GO; GO:0006355; P:regulation of transcription, DNA-dependent; IEA:UniProtKB-KW.
DR GO; GO:0006351; P:transcription, DNA-dependent; IEA:UniProtKB-KW.
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 3D-structure; Complete proteome; Cytoplasm; Direct protein sequencing;
KW Elongation factor; GTP-binding; Methylation; Nucleotide-binding;
KW Nucleus; Phosphoprotein; Protein biosynthesis; Reference proteome;
KW Transcription; Transcription regulation; Ubl conjugation.
FT CHAIN 1 462 Elongation factor 1-alpha 1.
FT /FTId=PRO_0000090885.
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.
FT MOD_RES 79 79 N6,N6,N6-trimethyllysine (By similarity).
FT MOD_RES 165 165 N6,N6-dimethyllysine.
FT MOD_RES 300 300 Phosphoserine; by TGFBR1.
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 432 432 Phosphothreonine; by PASK.
FT MUTAGEN 432 432 T->A: Abolishes phosphorylation by PASK.
FT CONFLICT 83 83 S -> A (in Ref. 6; CAA27325).
FT CONFLICT 232 232 L -> V (in Ref. 3; CAA34756).
FT STRAND 7 14
FT HELIX 20 31
FT TURN 34 36
FT HELIX 37 46
FT TURN 47 49
FT HELIX 51 53
FT HELIX 56 60
FT HELIX 61 63
FT TURN 64 66
FT STRAND 76 81
FT STRAND 86 91
FT HELIX 96 101
FT HELIX 103 106
FT STRAND 110 116
FT HELIX 124 127
FT HELIX 132 134
FT HELIX 136 143
FT STRAND 148 152
FT TURN 160 162
FT HELIX 164 166
FT HELIX 168 178
FT TURN 179 181
FT HELIX 185 187
FT STRAND 188 192
FT TURN 195 198
FT STRAND 199 203
FT STRAND 214 218
FT STRAND 221 227
FT HELIX 228 232
FT STRAND 243 245
FT STRAND 247 256
FT TURN 257 259
FT STRAND 260 265
FT STRAND 277 283
FT STRAND 286 293
FT STRAND 300 302
FT STRAND 309 314
FT TURN 317 319
FT STRAND 325 328
FT TURN 329 331
FT STRAND 337 346
FT STRAND 352 354
FT STRAND 360 363
FT STRAND 366 380
FT TURN 381 383
FT STRAND 392 395
FT STRAND 398 408
FT TURN 415 417
FT HELIX 419 422
FT STRAND 423 428
FT STRAND 431 442
SQ SEQUENCE 462 AA; 50141 MW; D465615545AF686A CRC64;
MGKEKTHINI VVIGHVDSGK STTTGHLIYK CGGIDKRTIE KFEKEAAEMG KGSFKYAWVL
DKLKAERERG ITIDISLWKF ETSKYYVTII DAPGHRDFIK NMITGTSQAD CAVLIVAAGV
GEFEAGISKN GQTREHALLA YTLGVKQLIV GVNKMDSTEP PYSQKRYEEI VKEVSTYIKK
IGYNPDTVAF VPISGWNGDN MLEPSANMPW FKGWKVTRKD GNASGTTLLE ALDCILPPTR
PTDKPLRLPL QDVYKIGGIG TVPVGRVETG VLKPGMVVTF APVNVTTEVK SVEMHHEALS
EALPGDNVGF NVKNVSVKDV RRGNVAGDSK NDPPMEAAGF TAQVIILNHP GQISAGYAPV
LDCHTAHIAC KFAELKEKID RRSGKKLEDG PKFLKSGDAA IVDMVPGKPM CVESFSDYPP
LGRFAVRDMR QTVAVGVIKA VDKKAAGAGK VTKSAQKAQK AK
//
MIM
130590
*RECORD*
*FIELD* NO
130590
*FIELD* TI
*130590 EUKARYOTIC TRANSLATION ELONGATION FACTOR 1, ALPHA-1; EEF1A1
;;ELONGATION FACTOR 1, ALPHA-1;;
read moreELONGATION FACTOR 1, ALPHA; EF1A; EEF1A
CERVICAL CANCER SUPPRESSOR 3 ISOFORM, INCLUDED; CCS3, INCLUDED
*FIELD* TX
DESCRIPTION
Eukaryotic elongation factor-1 (EF1) consists of 4 subunits, EF1-alpha,
EF1-beta (EEF1B2; 600655), EF1-gamma (EEF1G; 130593), and EF1-delta
(EEF1D; 130592). EIF-alpha-GTP transfers aminoacyl-tRNA to the ribosome,
and the release of animoacyl-tRNA from EIF-alpha-GTP is driven by GTP
hydrolysis. EF1-alpha-GDP is recycled to EF1-alpha-GTP by the EF1-beta,
-gamma, and -delta subunits (Sanders et al., 1996).
CLONING
Brands et al. (1986) determined the primary structure of human EEF1A by
cDNA sequencing. The deduced 462-amino acid protein shows conservation
of more than 80% when compared with yeast and Artema Ef1-alpha.
By immunofluorescence analysis, Sanders et al. (1996) found that
EF1-alpha showed strong nuclear staining and diffuse cytoplasmic
staining in human foreskin fibroblasts. In contrast, EF1-beta, -gamma,
and -delta showed a perinuclear distribution and colocalized with an
endoplasmic reticulum resident protein.
- CCS3 Splice Variant
Using PLZF (ZNF145; 176797) as bait in a yeast 2-hybrid screen of an
ovary cDNA library, Rho et al. (2006) cloned an EEF1A1 splice variant
that they called CCS3. The deduced 361-amino acid CCS3 protein lacks the
101 N-terminal amino acids of full-length EEF1A1. Western blot analysis
detected both CCS3 and full-length EEF1A1 in human cell lines.
GENE FUNCTION
Using human tissue culture cells, Morris et al. (2004) showed that
promoter-directed small interfering RNA (siRNA) inhibits transcription
of an integrated, proviral EF1A promoter-green fluorescent protein
reporter gene and of endogenous EF1A. Silencing was associated with DNA
methylation of the targeted sequence, and it required either active
transport of siRNA into the nucleus or permeabilization of the nuclear
envelope by lentiviral transduction. Morris et al. (2004) concluded that
siRNA-directed transcriptional silencing is conserved in mammals,
providing a means to inhibit mammalian gene function.
The heat-shock transcription factor HSF1 (140580) is present in
unstressed cells in an inactive monomeric form and becomes activated by
heat and other stress stimuli. HSF1 activation involves trimerization
and acquisition of a site-specific DNA-binding activity, which is
negatively regulated by interaction with certain heat-shock proteins.
Shamovsky et al. (2006) showed that HSF1 activation by heat shock is an
active process that is mediated by a ribonucleoprotein complex
containing translation elongation factor eEF1A and a previously unknown
noncoding RNA that they termed heat-shock RNA-1 (HSR1; 610157). HSR1 is
constitutively expressed in human and rodent cells and its homologs are
functionally interchangeable. Both HSR1 and eEF1A are required for HSF1
activation in vitro; antisense oligonucleotides or short interfering RNA
against HSR1 impaired the heat-shock response in vivo, rendering cells
thermosensitive. Shamovsky et al. (2006) suggested that the central role
of HSR1 during heat shock implies that targeting this RNA could serve as
a new therapeutic model for cancer, inflammation, and other conditions
associated with HSF1 deregulation.
Using mass spectrometric analysis, Belyi et al. (2006) identified EF1A
as the protein glucosylated after infection with Legionella pneumophila,
the causative agent of Legionnaire disease (see 608556). Glucosylation
occurs at ser53 in the GTPase domain of EF1A and results in inhibition
of eukaryotic protein synthesis and target cell death.
- CCS3 Isoform
Using yeast 2-hybrid analysis and protein pull-down assays, Rho et al.
(2006) showed that CCS3 interacted with PLZF. Mutation analysis revealed
that repressor domain-2 and the zinc finger domain of PLZF were required
for the interaction. RT-PCR showed that CCS3 was downregulated in human
cervical cancer cell lines and in 7 of 8 human cervical cancers compared
with normal human cell lines and tissues. Overexpression of CCS3
inhibited cell growth by inducing apoptosis, and CCS3 suppressed human
cyclin A2 (CCNA2; 123835) promoter activity in a reporter gene assay.
Rho et al. (2006) concluded that CCS3 functions as a transcriptional
repressor and is required for the transcriptional effects of PLZF.
BIOCHEMICAL FEATURES
Ditzel et al. (2000) identified EEF1A1 as an autoantibody in 66% of
patients with Felty syndrome (134750), a disorder characterized by the
association of rheumatoid arthritis, splenomegaly, and peripheral
destruction of neutrophils leading to neutropenia.
MAPPING
Opdenakker et al. (1987) concluded that there are more than 10 copies
per haploid genome of EEF1A in humans. Using in situ hybridization of a
cDNA probe to normal metaphase chromosomes, they showed multiple
chromosomal localizations of the elongation factor genes, with peak
hybridization on chromosomes 1, 2, 4, 5, 6, 7, and 15.
By fluorescence in situ hybridization (FISH) and PCR analysis of a
somatic cell hybrid panel, Lund et al. (1996) mapped the EEF1A1 gene to
chromosome 6q14. By FISH, they mapped the EEF1A2 gene (602959) to
20q13.3.
*FIELD* RF
1. Belyi, Y.; Niggeweg, R.; Opitz, B.; Vogelsgesang, M.; Hippenstiel,
S.; Wilm, M.; Aktories, K.: Legionella pneumophila glucosyltransferase
inhibits host elongation factor 1A. Proc. Nat. Acad. Sci. 103: 16953-16958,
2006.
2. Brands, J. H. G. M.; Maassen, J. A.; Van Hemert, F. J.; Amons,
R.; Moller, W.: The primary structure of the alpha subunit of human
elongation factor 1: structural aspects of guanine-nucleotide-binding
sites. Europ. J. Biochem. 155: 167-171, 1986.
3. Ditzel, H. J.; Masaki, Y.; Nielsen, H.; Farnaes, L.; Burton, D.
R.: Cloning and expression of a novel human antibody--antigen pair
associated with Felty's syndrome. Proc. Nat. Acad. Sci. 97: 9234-9239,
2000.
4. Lund, A.; Knudsen, S. M.; Vissing, H.; Clark, B.; Tommerup, N.
: Assignment of human elongation factor 1-alpha genes: EEF1A maps
to chromosome 6q14 and EEF1A2 to 20q13.3. Genomics 36: 359-361,
1996.
5. Morris, K. V.; Chan, S. W.-L.; Jacobsen, S. E.; Looney, D. J.:
Small interfering RNA-induced transcriptional gene silencing in human
cells. Science 305: 1289-1292, 2004.
6. Opdenakker, G.; Cabeza-Arvelaiz, Y.; Fiten, P.; Dijkmans, R.; Van
Damme, J.; Volckaert, G.; Billiau, A.; Van Elsen, A.; Van der Schueren,
B.; Van den Berghe, H.; Cassiman, J.-J.: Human elongation factor
1-alpha: a polymorphic and conserved multigene family with multiple
chromosomal localizations. Hum. Genet. 75: 339-344, 1987.
7. Rho, S. B.; Park, Y. G.; Park, K.; Lee, S.-H.; Lee, J.-H.: A novel
cervical cancer suppressor 3 (CCS-3) interacts with the BTB domain
of PLZF and inhibits the cell growth by inducing apoptosis. FEBS
Lett. 580: 4073-4080, 2006.
8. Sanders, J.; Brandsma, M.; Janssen, G. M. C.; Dijk, J.; Moller,
W.: Immunofluorescence studies of human fibroblasts demonstrate the
presence of the complex of elongation factor-1-beta-gamma-delta in
the endoplasmic reticulum. J. Cell Sci. 109: 1113-1117, 1996.
9. Shamovsky, I.; Ivannikov, M.; Kandel, E. S.; Gershon, D.; Nudler,
E.: RNA-mediated response to heat shock in mammalian cells. Nature 440:
556-560, 2006.
*FIELD* CN
Patricia A. Hartz - updated: 10/3/2008
Patricia A. Hartz - updated: 11/29/2007
Paul J. Converse - updated: 1/17/2007
Ada Hamosh - updated: 5/26/2006
Ada Hamosh - updated: 10/5/2004
Carol A. Bocchini - updated: 8/11/1998
*FIELD* CD
Victor A. McKusick: 6/24/1986
*FIELD* ED
joanna: 07/27/2010
mgross: 10/8/2008
terry: 10/3/2008
mgross: 11/30/2007
terry: 11/29/2007
mgross: 1/17/2007
alopez: 6/2/2006
terry: 5/26/2006
tkritzer: 10/5/2004
terry: 10/5/2004
mcapotos: 10/9/2000
carol: 8/11/1998
terry: 8/11/1998
carol: 8/11/1998
dkim: 6/30/1998
mark: 5/9/1995
supermim: 3/16/1992
supermim: 3/20/1990
ddp: 10/26/1989
marie: 3/25/1988
root: 1/11/1988
*RECORD*
*FIELD* NO
130590
*FIELD* TI
*130590 EUKARYOTIC TRANSLATION ELONGATION FACTOR 1, ALPHA-1; EEF1A1
;;ELONGATION FACTOR 1, ALPHA-1;;
read moreELONGATION FACTOR 1, ALPHA; EF1A; EEF1A
CERVICAL CANCER SUPPRESSOR 3 ISOFORM, INCLUDED; CCS3, INCLUDED
*FIELD* TX
DESCRIPTION
Eukaryotic elongation factor-1 (EF1) consists of 4 subunits, EF1-alpha,
EF1-beta (EEF1B2; 600655), EF1-gamma (EEF1G; 130593), and EF1-delta
(EEF1D; 130592). EIF-alpha-GTP transfers aminoacyl-tRNA to the ribosome,
and the release of animoacyl-tRNA from EIF-alpha-GTP is driven by GTP
hydrolysis. EF1-alpha-GDP is recycled to EF1-alpha-GTP by the EF1-beta,
-gamma, and -delta subunits (Sanders et al., 1996).
CLONING
Brands et al. (1986) determined the primary structure of human EEF1A by
cDNA sequencing. The deduced 462-amino acid protein shows conservation
of more than 80% when compared with yeast and Artema Ef1-alpha.
By immunofluorescence analysis, Sanders et al. (1996) found that
EF1-alpha showed strong nuclear staining and diffuse cytoplasmic
staining in human foreskin fibroblasts. In contrast, EF1-beta, -gamma,
and -delta showed a perinuclear distribution and colocalized with an
endoplasmic reticulum resident protein.
- CCS3 Splice Variant
Using PLZF (ZNF145; 176797) as bait in a yeast 2-hybrid screen of an
ovary cDNA library, Rho et al. (2006) cloned an EEF1A1 splice variant
that they called CCS3. The deduced 361-amino acid CCS3 protein lacks the
101 N-terminal amino acids of full-length EEF1A1. Western blot analysis
detected both CCS3 and full-length EEF1A1 in human cell lines.
GENE FUNCTION
Using human tissue culture cells, Morris et al. (2004) showed that
promoter-directed small interfering RNA (siRNA) inhibits transcription
of an integrated, proviral EF1A promoter-green fluorescent protein
reporter gene and of endogenous EF1A. Silencing was associated with DNA
methylation of the targeted sequence, and it required either active
transport of siRNA into the nucleus or permeabilization of the nuclear
envelope by lentiviral transduction. Morris et al. (2004) concluded that
siRNA-directed transcriptional silencing is conserved in mammals,
providing a means to inhibit mammalian gene function.
The heat-shock transcription factor HSF1 (140580) is present in
unstressed cells in an inactive monomeric form and becomes activated by
heat and other stress stimuli. HSF1 activation involves trimerization
and acquisition of a site-specific DNA-binding activity, which is
negatively regulated by interaction with certain heat-shock proteins.
Shamovsky et al. (2006) showed that HSF1 activation by heat shock is an
active process that is mediated by a ribonucleoprotein complex
containing translation elongation factor eEF1A and a previously unknown
noncoding RNA that they termed heat-shock RNA-1 (HSR1; 610157). HSR1 is
constitutively expressed in human and rodent cells and its homologs are
functionally interchangeable. Both HSR1 and eEF1A are required for HSF1
activation in vitro; antisense oligonucleotides or short interfering RNA
against HSR1 impaired the heat-shock response in vivo, rendering cells
thermosensitive. Shamovsky et al. (2006) suggested that the central role
of HSR1 during heat shock implies that targeting this RNA could serve as
a new therapeutic model for cancer, inflammation, and other conditions
associated with HSF1 deregulation.
Using mass spectrometric analysis, Belyi et al. (2006) identified EF1A
as the protein glucosylated after infection with Legionella pneumophila,
the causative agent of Legionnaire disease (see 608556). Glucosylation
occurs at ser53 in the GTPase domain of EF1A and results in inhibition
of eukaryotic protein synthesis and target cell death.
- CCS3 Isoform
Using yeast 2-hybrid analysis and protein pull-down assays, Rho et al.
(2006) showed that CCS3 interacted with PLZF. Mutation analysis revealed
that repressor domain-2 and the zinc finger domain of PLZF were required
for the interaction. RT-PCR showed that CCS3 was downregulated in human
cervical cancer cell lines and in 7 of 8 human cervical cancers compared
with normal human cell lines and tissues. Overexpression of CCS3
inhibited cell growth by inducing apoptosis, and CCS3 suppressed human
cyclin A2 (CCNA2; 123835) promoter activity in a reporter gene assay.
Rho et al. (2006) concluded that CCS3 functions as a transcriptional
repressor and is required for the transcriptional effects of PLZF.
BIOCHEMICAL FEATURES
Ditzel et al. (2000) identified EEF1A1 as an autoantibody in 66% of
patients with Felty syndrome (134750), a disorder characterized by the
association of rheumatoid arthritis, splenomegaly, and peripheral
destruction of neutrophils leading to neutropenia.
MAPPING
Opdenakker et al. (1987) concluded that there are more than 10 copies
per haploid genome of EEF1A in humans. Using in situ hybridization of a
cDNA probe to normal metaphase chromosomes, they showed multiple
chromosomal localizations of the elongation factor genes, with peak
hybridization on chromosomes 1, 2, 4, 5, 6, 7, and 15.
By fluorescence in situ hybridization (FISH) and PCR analysis of a
somatic cell hybrid panel, Lund et al. (1996) mapped the EEF1A1 gene to
chromosome 6q14. By FISH, they mapped the EEF1A2 gene (602959) to
20q13.3.
*FIELD* RF
1. Belyi, Y.; Niggeweg, R.; Opitz, B.; Vogelsgesang, M.; Hippenstiel,
S.; Wilm, M.; Aktories, K.: Legionella pneumophila glucosyltransferase
inhibits host elongation factor 1A. Proc. Nat. Acad. Sci. 103: 16953-16958,
2006.
2. Brands, J. H. G. M.; Maassen, J. A.; Van Hemert, F. J.; Amons,
R.; Moller, W.: The primary structure of the alpha subunit of human
elongation factor 1: structural aspects of guanine-nucleotide-binding
sites. Europ. J. Biochem. 155: 167-171, 1986.
3. Ditzel, H. J.; Masaki, Y.; Nielsen, H.; Farnaes, L.; Burton, D.
R.: Cloning and expression of a novel human antibody--antigen pair
associated with Felty's syndrome. Proc. Nat. Acad. Sci. 97: 9234-9239,
2000.
4. Lund, A.; Knudsen, S. M.; Vissing, H.; Clark, B.; Tommerup, N.
: Assignment of human elongation factor 1-alpha genes: EEF1A maps
to chromosome 6q14 and EEF1A2 to 20q13.3. Genomics 36: 359-361,
1996.
5. Morris, K. V.; Chan, S. W.-L.; Jacobsen, S. E.; Looney, D. J.:
Small interfering RNA-induced transcriptional gene silencing in human
cells. Science 305: 1289-1292, 2004.
6. Opdenakker, G.; Cabeza-Arvelaiz, Y.; Fiten, P.; Dijkmans, R.; Van
Damme, J.; Volckaert, G.; Billiau, A.; Van Elsen, A.; Van der Schueren,
B.; Van den Berghe, H.; Cassiman, J.-J.: Human elongation factor
1-alpha: a polymorphic and conserved multigene family with multiple
chromosomal localizations. Hum. Genet. 75: 339-344, 1987.
7. Rho, S. B.; Park, Y. G.; Park, K.; Lee, S.-H.; Lee, J.-H.: A novel
cervical cancer suppressor 3 (CCS-3) interacts with the BTB domain
of PLZF and inhibits the cell growth by inducing apoptosis. FEBS
Lett. 580: 4073-4080, 2006.
8. Sanders, J.; Brandsma, M.; Janssen, G. M. C.; Dijk, J.; Moller,
W.: Immunofluorescence studies of human fibroblasts demonstrate the
presence of the complex of elongation factor-1-beta-gamma-delta in
the endoplasmic reticulum. J. Cell Sci. 109: 1113-1117, 1996.
9. Shamovsky, I.; Ivannikov, M.; Kandel, E. S.; Gershon, D.; Nudler,
E.: RNA-mediated response to heat shock in mammalian cells. Nature 440:
556-560, 2006.
*FIELD* CN
Patricia A. Hartz - updated: 10/3/2008
Patricia A. Hartz - updated: 11/29/2007
Paul J. Converse - updated: 1/17/2007
Ada Hamosh - updated: 5/26/2006
Ada Hamosh - updated: 10/5/2004
Carol A. Bocchini - updated: 8/11/1998
*FIELD* CD
Victor A. McKusick: 6/24/1986
*FIELD* ED
joanna: 07/27/2010
mgross: 10/8/2008
terry: 10/3/2008
mgross: 11/30/2007
terry: 11/29/2007
mgross: 1/17/2007
alopez: 6/2/2006
terry: 5/26/2006
tkritzer: 10/5/2004
terry: 10/5/2004
mcapotos: 10/9/2000
carol: 8/11/1998
terry: 8/11/1998
carol: 8/11/1998
dkim: 6/30/1998
mark: 5/9/1995
supermim: 3/16/1992
supermim: 3/20/1990
ddp: 10/26/1989
marie: 3/25/1988
root: 1/11/1988