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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)

 EF1A1_HUMAN             Reviewed;         462 AA.
P68104; P04719; P04720; Q6IQ15;
13-AUG-1987, integrated into UniProtKB/Swiss-Prot.
13-AUG-1987, sequence version 1.
07-NOV-2018, entry version 174.
RecName: Full=Elongation factor 1-alpha 1;
Short=EF-1-alpha-1;
AltName: Full=Elongation factor Tu;
Short=EF-Tu;
AltName: Full=Eukaryotic elongation factor 1 A-1;
Short=eEF1A-1;
AltName: Full=Leukocyte receptor cluster member 7;
Name=EEF1A1; Synonyms=EEF1A, EF1A, LENG7;
Homo sapiens (Human).
Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
Catarrhini; Hominidae; Homo.
NCBI_TaxID=9606;
[1]
NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1).
PubMed=3512269; DOI=10.1111/j.1432-1033.1986.tb09472.x;
Brands J.H.G.M., Maassen J.A., van Hemert F.J., Amons R., Moeller W.;
"The primary structure of the alpha subunit of human elongation factor
1. Structural aspects of guanine-nucleotide-binding sites.";
Eur. J. Biochem. 155:167-171(1986).
[2]
NUCLEOTIDE SEQUENCE [GENOMIC DNA].
PubMed=2564392;
Uetsuki T., Naito A., Nagata S., Kaziro Y.;
"Isolation and characterization of the human chromosomal gene for
polypeptide chain elongation factor-1 alpha.";
J. Biol. Chem. 264:5791-5798(1989).
[3]
NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1).
TISSUE=Liver;
PubMed=2183196; DOI=10.1093/nar/18.6.1513;
Madsen H.O., Poulsen K., Dahl O., Clark B.F.C., Hjorth J.P.;
"Retropseudogenes constitute the major part of the human elongation
factor 1 alpha gene family.";
Nucleic Acids Res. 18:1513-1516(1990).
[4]
NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1).
Shimazu T., Koike K.;
"Postnatal expression of a novel mRNA isoform from the human
elongation factor-1a gene.";
Submitted (JUL-2001) to the EMBL/GenBank/DDBJ databases.
[5]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 1 AND 2).
TISSUE=B-cell, Bone marrow, Cervix, Colon, Hippocampus, Kidney, Lung,
Lymph, Mammary gland, Ovary, Pancreas, Placenta, Testis, and Uterus;
PubMed=15489334; DOI=10.1101/gr.2596504;
The MGC Project Team;
"The status, quality, and expansion of the NIH full-length cDNA
project: the Mammalian Gene Collection (MGC).";
Genome Res. 14:2121-2127(2004).
[6]
NUCLEOTIDE SEQUENCE [MRNA] OF 1-94 (ISOFORM 1/2).
PubMed=3960725; DOI=10.1093/nar/14.5.2409;
Rao T.R., Slobin L.I.;
"Structure of the amino-terminal end of mammalian elongation factor
Tu.";
Nucleic Acids Res. 14:2409-2409(1986).
[7]
PROTEIN SEQUENCE OF 6-30; 52-62; 85-96; 101-129; 135-180; 248-313;
396-423 AND 431-439, METHYLATION AT LYS-55 AND LYS-165, AND
IDENTIFICATION BY MASS SPECTROMETRY.
TISSUE=Colon carcinoma, and Ovarian carcinoma;
Bienvenut W.V., Zebisch A., Kolch W.;
Submitted (JAN-2010) to UniProtKB.
[8]
PROTEIN SEQUENCE OF 7-16 AND 85-96, INTERACTION WITH PARP1 AND TXK,
PHOSPHORYLATION BY TXK, SUBCELLULAR LOCATION, AND FUNCTION AS A
TRANSCRIPTION FACTOR.
PubMed=17177976; DOI=10.1111/j.1365-2249.2006.03249.x;
Maruyama T., Nara K., Yoshikawa H., Suzuki N.;
"Txk, a member of the non-receptor tyrosine kinase of the Tec family,
forms a complex with poly(ADP-ribose) polymerase 1 and elongation
factor 1alpha and regulates interferon-gamma gene transcription in Th1
cells.";
Clin. Exp. Immunol. 147:164-175(2007).
[9]
PROTEIN SEQUENCE OF 38-44; 70-79; 85-96; 135-172; 248-290; 386-392 AND
428-439.
TISSUE=B-cell lymphoma;
Bienvenut W.V.;
Submitted (JUN-2005) to UniProtKB.
[10]
NUCLEOTIDE SEQUENCE [MRNA] OF 138-462 (ISOFORM 1).
PubMed=3346208;
Ann D.K., Wu M.M.J., Huang T., Carlson D.M., Wu R.;
"Retinol-regulated gene expression in human tracheobronchial
epithelial cells. Enhanced expression of elongation factor EF-1
alpha.";
J. Biol. Chem. 263:3546-3549(1988).
[11]
ETHANOLAMINYLATION AT GLU-301 AND GLU-374.
PubMed=2569467;
Whiteheart S.W., Shenbagarmurthi P., Chen L., Cotter R.J., Hart G.W.;
"Murine elongation factor 1 alpha (EF-1 alpha) is posttranslationally
modified by novel amide-linked ethanolamine-phosphoglycerol moieties.
Addition of ethanolamine-phosphoglycerol to specific glutamic acid
residues on EF-1 alpha.";
J. Biol. Chem. 264:14334-14341(1989).
[12]
INTERACTION WITH ZPR1, AND SUBCELLULAR LOCATION.
PubMed=8650580; DOI=10.1126/science.272.5269.1797;
Galcheva-Gargova Z., Konstantinov K.N., Wu I.-H., Klier F.G.,
Barrett T., Davis R.J.;
"Binding of zinc finger protein ZPR1 to the epidermal growth factor
receptor.";
Science 272:1797-1802(1996).
[13]
INDUCTION BY HOMOCYSTEINE.
PubMed=9677419; DOI=10.1074/jbc.273.31.19840;
Chacko G., Ling Q., Hajjar K.A.;
"Induction of acute translational response genes by homocysteine.
Elongation factors-1alpha, -beta, and -delta.";
J. Biol. Chem. 273:19840-19846(1998).
[14]
IDENTIFICATION IN A NUCLEAR EXPORT RECEPTOR COMPLEX WITH XPO5; RAN AND
TRNA, AND INTERACTION WITH XPO5.
PubMed=12426392; DOI=10.1093/emboj/cdf613;
Bohnsack M.T., Regener K., Schwappach B., Saffrich R., Paraskeva E.,
Hartmann E., Goerlich D.;
"Exp5 exports eEF1A via tRNA from nuclei and synergizes with other
transport pathways to confine translation to the cytoplasm.";
EMBO J. 21:6205-6215(2002).
[15]
IDENTIFICATION IN A NUCLEAR EXPORT RECEPTOR COMPLEX WITH XPO5; RAN AND
TRNA, AND INTERACTION WITH XPO5.
PubMed=12426393; DOI=10.1093/emboj/cdf620;
Calado A., Treichel N., Mueller E.-C., Otto A., Kutay U.;
"Exportin-5-mediated nuclear export of eukaryotic elongation factor 1A
and tRNA.";
EMBO J. 21:6216-6224(2002).
[16]
ISGYLATION.
PubMed=16139798; DOI=10.1016/j.bbrc.2005.08.132;
Giannakopoulos N.V., Luo J.K., Papov V., Zou W., Lenschow D.J.,
Jacobs B.S., Borden E.C., Li J., Virgin H.W., Zhang D.E.;
"Proteomic identification of proteins conjugated to ISG15 in mouse and
human cells.";
Biochem. Biophys. Res. Commun. 336:496-506(2005).
[17]
PHOSPHORYLATION AT THR-432, AND MUTAGENESIS OF THR-432.
PubMed=17595531; DOI=10.1159/000104169;
Eckhardt K., Troger J., Reissmann J., Katschinski D.M., Wagner K.F.,
Stengel P., Paasch U., Hunziker P., Borter E., Barth S., Schlafli P.,
Spielmann P., Stiehl D.P., Camenisch G., Wenger R.H.;
"Male germ cell expression of the PAS domain kinase PASKIN and its
novel target eukaryotic translation elongation factor eEF1A1.";
Cell. Physiol. Biochem. 20:227-240(2007).
[18]
INTERACTION WITH KARS.
PubMed=18029264; DOI=10.1016/j.bbrc.2007.11.028;
Guzzo C.M., Yang D.C.H.;
"Lysyl-tRNA synthetase interacts with EF1alpha, aspartyl-tRNA
synthetase and p38 in vitro.";
Biochem. Biophys. Res. Commun. 365:718-723(2008).
[19]
INTERACTION WITH ERGIC2.
PubMed=17980171; DOI=10.1016/j.bbapap.2007.10.006;
Yang Y.F., Chou M.Y., Fan C.Y., Chen S.F., Lyu P.C., Liu C.C.,
Tseng T.L.;
"The possible interaction of CDA14 and protein elongation factor
1alpha.";
Biochim. Biophys. Acta 1784:312-318(2008).
[20]
INTERACTION WITH DLC1, AND SUBCELLULAR LOCATION.
PubMed=19158340; DOI=10.1242/jcs.027482;
Zhong D., Zhang J., Yang S., Soh U.J., Buschdorf J.P., Zhou Y.T.,
Yang D., Low B.C.;
"The SAM domain of the RhoGAP DLC1 binds EF1A1 to regulate cell
migration.";
J. Cell Sci. 122:414-424(2009).
[21]
PHOSPHORYLATION AT SER-300.
PubMed=20832312; DOI=10.1016/j.cub.2010.08.017;
Lin K.W., Yakymovych I., Jia M., Yakymovych M., Souchelnytskyi S.;
"Phosphorylation of eEF1A1 at Ser300 by TbetaR-I results in inhibition
of mRNA translation.";
Curr. Biol. 20:1615-1625(2010).
[22]
METHYLATION AT LYS-318, AND MUTAGENESIS OF LYS-36; LYS-55; LYS-79;
LYS-165 AND LYS-318.
PubMed=25144183; DOI=10.1371/journal.pone.0105394;
Shimazu T., Barjau J., Sohtome Y., Sodeoka M., Shinkai Y.;
"Selenium-based S-adenosylmethionine analog reveals the mammalian
seven-beta-strand methyltransferase METTL10 to be an EF1A1 lysine
methyltransferase.";
PLoS ONE 9:E105394-E105394(2014).
[23]
SUBCELLULAR LOCATION, INTERACTION WITH PPP1R16B, AND PHOSPHORYLATION
BY ROCK2.
PubMed=26497934; DOI=10.1016/j.biocel.2015.10.021;
Boratko A., Peter M., Thalwieser Z., Kovacs E., Csortos C.;
"Elongation factor-1A1 is a novel substrate of the protein phosphatase
1-TIMAP complex.";
Int. J. Biochem. Cell Biol. 69:105-113(2015).
[24]
METHYLATION AT GLY-2 AND LYS-79.
PubMed=26545399; DOI=10.1074/mcp.M115.052449;
Hamey J.J., Winter D.L., Yagoub D., Overall C.M., Hart-Smith G.,
Wilkins M.R.;
"Novel N-terminal and lysine methyltransferases that target
translation elongation factor 1A in yeast and human.";
Mol. Cell. Proteomics 15:164-176(2016).
[25]
METHYLATION AT LYS-165, AND MUTAGENESIS OF LYS-165.
PubMed=28108655; DOI=10.1093/nar/gkx002;
Malecki J., Aileni V.K., Ho A.Y., Schwarz J., Moen A., Soerensen V.,
Nilges B.S., Jakobsson M.E., Leidel S.A., Falnes P.O.;
"The novel lysine specific methyltransferase METTL21B affects mRNA
translation through inducible and dynamic methylation of Lys-165 in
human eukaryotic elongation factor 1 alpha (eEF1A).";
Nucleic Acids Res. 45:4370-4389(2017).
[26]
METHYLATION AT LYS-36, IDENTIFICATION BY MASS SPECTROMETRY, AND
MUTAGENESIS OF LYS-36.
PubMed=28520920; DOI=10.1093/nar/gkx432;
Jakobsson M.E., Malecki J., Nilges B.S., Moen A., Leidel S.A.,
Falnes P.O.;
"Methylation of human eukaryotic elongation factor alpha (eEF1A) by a
member of a novel protein lysine methyltransferase family modulates
mRNA translation.";
Nucleic Acids Res. 45:8239-8254(2017).
-!- FUNCTION: This protein promotes the GTP-dependent binding of
aminoacyl-tRNA to the A-site of ribosomes during protein
biosynthesis. With PARP1 and TXK, forms a complex that acts as a T
helper 1 (Th1) cell-specific transcription factor and binds the
promoter of IFN-gamma to directly regulate its transcription, and
is thus involved importantly in Th1 cytokine production.
{ECO:0000269|PubMed:17177976}.
-!- SUBUNIT: Found in a nuclear export complex with XPO5, EEF1A1, Ran
and aminoacylated tRNA. Interacts with PARP1, TXK, XPO5 and KARS.
May interact with ERGIC2. Interacts with IFIT1 (via TPR repeats 4-
7) (By similarity). Interacts with DLC1, facilitating distribution
to the membrane periphery and ruffles upon growth factor
stimulation. Interacts with ZPR1; the interaction occurs in a
epidermal growth factor (EGF)-dependent manner. Interacts with
PPP1R16B (PubMed:26497934). {ECO:0000250,
ECO:0000269|PubMed:12426392, ECO:0000269|PubMed:12426393,
ECO:0000269|PubMed:17177976, ECO:0000269|PubMed:17980171,
ECO:0000269|PubMed:18029264, ECO:0000269|PubMed:19158340,
ECO:0000269|PubMed:26497934, ECO:0000269|PubMed:8650580}.
-!- INTERACTION:
Q8NFJ9:BBS1; NbExp=3; IntAct=EBI-352162, EBI-1805484;
Q00987:MDM2; NbExp=9; IntAct=EBI-352162, EBI-389668;
P54725:RAD23A; NbExp=2; IntAct=EBI-352162, EBI-746453;
Q9NYA1:SPHK1; NbExp=2; IntAct=EBI-352162, EBI-985303;
P63104:YWHAZ; NbExp=2; IntAct=EBI-352162, EBI-347088;
Q05516:ZBTB16; NbExp=4; IntAct=EBI-352162, EBI-711925;
Q8IUH5:ZDHHC17; NbExp=2; IntAct=EBI-352162, EBI-524753;
-!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000269|PubMed:19158340,
ECO:0000269|PubMed:8650580}. Nucleus {ECO:0000269|PubMed:17177976,
ECO:0000269|PubMed:8650580}. Nucleus, nucleolus
{ECO:0000269|PubMed:8650580}. Cell membrane
{ECO:0000269|PubMed:26497934}. Note=Colocalizes with DLC1 at
actin-rich regions in the cell periphery (PubMed:19158340).
Translocates together with ZPR1 from the cytoplasm to the nucleus
and nucleolus after treatment with mitogens (PubMed:8650580).
Localization at the cell membrane depends on EEF1A1
phosphorylation status and the presence of PPP1R16B
(PubMed:26497934). {ECO:0000269|PubMed:19158340,
ECO:0000269|PubMed:26497934, ECO:0000269|PubMed:8650580}.
-!- ALTERNATIVE PRODUCTS:
Event=Alternative splicing; Named isoforms=2;
Name=1;
IsoId=P68104-1; Sequence=Displayed;
Name=2;
IsoId=P68104-2; Sequence=VSP_057184;
Note=No experimental confirmation available.;
-!- TISSUE SPECIFICITY: Brain, placenta, lung, liver, kidney, pancreas
but barely detectable in heart and skeletal muscle.
-!- INDUCTION: By homocysteine (HC), may mediate accelerated synthesis
of free thiol-containing proteins in response to HC-induced
oxidative stress. {ECO:0000269|PubMed:9677419}.
-!- PTM: ISGylated. {ECO:0000269|PubMed:16139798}.
-!- PTM: Phosphorylated by TXK. Phosphorylation by PASK increases
translation efficiency. Phosphorylated by ROCK2 (PubMed:26497934).
{ECO:0000269|PubMed:17177976, ECO:0000269|PubMed:17595531,
ECO:0000269|PubMed:20832312, ECO:0000269|PubMed:26497934}.
-!- PTM: Trimethylated at Lys-79 by EEF1AKMT1 (PubMed:26545399).
Methylated at Lys-165 by EEF1AKMT3, methylation by EEF1AKMT3 is
dynamic as well as inducible by stress conditions, such as ER-
stress, and plays a regulatory role on mRNA translation
(PubMed:28108655). Trimethylated at Lys-318 by EEF1AKMT2
(PubMed:25144183). Mono-, di-, and trimethylated at Lys-36 by
EEF1AKMT4; trimethylated form is predominant. Methylation by
EEF1AKMT4 contributes to the fine-tuning of translation rates for
a subset of tRNAs (PubMed:28520920). {ECO:0000269|PubMed:25144183,
ECO:0000269|PubMed:26545399, ECO:0000269|PubMed:28108655,
ECO:0000269|PubMed:28520920}.
-!- SIMILARITY: Belongs to the TRAFAC class translation factor GTPase
superfamily. Classic translation factor GTPase family. EF-Tu/EF-1A
subfamily. {ECO:0000305}.
-!- SEQUENCE CAUTION:
Sequence=AAA52367.1; Type=Erroneous initiation; Note=Translation N-terminally shortened.; Evidence={ECO:0000305};
-!- WEB RESOURCE: Name=Atlas of Genetics and Cytogenetics in Oncology
and Haematology;
URL="http://atlasgeneticsoncology.org/Genes/EEF1A1ID40407ch6q13.html";
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EMBL; X03558; CAA27245.1; -; mRNA.
EMBL; J04617; AAA52343.1; -; Genomic_DNA.
EMBL; X16869; CAA34756.1; -; mRNA.
EMBL; AY043301; AAK95378.1; -; mRNA.
EMBL; BC008587; AAH08587.1; -; mRNA.
EMBL; BC009733; AAH09733.1; -; mRNA.
EMBL; BC009875; AAH09875.1; -; mRNA.
EMBL; BC010735; AAH10735.1; -; mRNA.
EMBL; BC012891; AAH12891.1; -; mRNA.
EMBL; BC014224; AAH14224.1; -; mRNA.
EMBL; BC018150; AAH18150.1; -; mRNA.
EMBL; BC018641; AAH18641.1; -; mRNA.
EMBL; BC021686; AAH21686.1; -; mRNA.
EMBL; BC028674; AAH28674.1; -; mRNA.
EMBL; BC038339; AAH38339.1; -; mRNA.
EMBL; BC057391; AAH57391.1; -; mRNA.
EMBL; BC066893; AAH66893.1; -; mRNA.
EMBL; BC071619; AAH71619.1; -; mRNA.
EMBL; BC072385; AAH72385.1; -; mRNA.
EMBL; BC082268; AAH82268.1; -; mRNA.
EMBL; X03689; CAA27325.1; -; mRNA.
EMBL; M29548; AAA52367.1; ALT_INIT; mRNA.
CCDS; CCDS4980.1; -. [P68104-1]
PIR; B24977; EFHU1.
RefSeq; NP_001393.1; NM_001402.5. [P68104-1]
RefSeq; XP_011533816.1; XM_011535514.2.
UniGene; Hs.535192; -.
UniGene; Hs.586423; -.
UniGene; Hs.745122; -.
PDB; 1SYW; Model; -; A=2-443.
PDB; 3C5J; X-ray; 1.80 A; C=343-355.
PDBsum; 1SYW; -.
PDBsum; 3C5J; -.
ProteinModelPortal; P68104; -.
SMR; P68104; -.
BioGrid; 108237; 406.
CORUM; P68104; -.
DIP; DIP-31277N; -.
IntAct; P68104; 190.
MINT; P68104; -.
STRING; 9606.ENSP00000330054; -.
BindingDB; P68104; -.
ChEMBL; CHEMBL1795120; -.
DrugBank; DB04315; Guanosine-5'-Diphosphate.
MoonProt; P68104; -.
iPTMnet; P68104; -.
PhosphoSitePlus; P68104; -.
SwissPalm; P68104; -.
BioMuta; EEF1A1; -.
DMDM; 55584035; -.
OGP; P68104; -.
SWISS-2DPAGE; P68104; -.
UCD-2DPAGE; P68104; -.
EPD; P68104; -.
PaxDb; P68104; -.
PeptideAtlas; P68104; -.
PRIDE; P68104; -.
ProteomicsDB; 57529; -.
DNASU; 1915; -.
Ensembl; ENST00000309268; ENSP00000339053; ENSG00000156508. [P68104-1]
Ensembl; ENST00000316292; ENSP00000339063; ENSG00000156508. [P68104-1]
Ensembl; ENST00000331523; ENSP00000330054; ENSG00000156508. [P68104-1]
GeneID; 1915; -.
KEGG; hsa:1915; -.
CTD; 1915; -.
DisGeNET; 1915; -.
EuPathDB; HostDB:ENSG00000156508.17; -.
GeneCards; EEF1A1; -.
H-InvDB; HIX0020005; -.
H-InvDB; HIX0032108; -.
H-InvDB; HIX0033669; -.
H-InvDB; HIX0169110; -.
HGNC; HGNC:3189; EEF1A1.
HPA; HPA051759; -.
HPA; HPA053862; -.
HPA; HPA056990; -.
MIM; 130590; gene.
neXtProt; NX_P68104; -.
OpenTargets; ENSG00000156508; -.
PharmGKB; PA27625; -.
eggNOG; KOG0052; Eukaryota.
eggNOG; COG5256; LUCA.
GeneTree; ENSGT00910000144046; -.
HOGENOM; HOG000229291; -.
HOVERGEN; HBG000179; -.
InParanoid; P68104; -.
KO; K03231; -.
OMA; PAKETKM; -.
OrthoDB; EOG091G05LW; -.
PhylomeDB; P68104; -.
TreeFam; TF300304; -.
Reactome; R-HSA-156842; Eukaryotic Translation Elongation.
Reactome; R-HSA-156902; Peptide chain elongation.
Reactome; R-HSA-3371511; HSF1 activation.
Reactome; R-HSA-6798695; Neutrophil degranulation.
Reactome; R-HSA-8876725; Protein methylation.
SignaLink; P68104; -.
SIGNOR; P68104; -.
ChiTaRS; EEF1A1; human.
GeneWiki; Eukaryotic_translation_elongation_factor_1_alpha_1; -.
GenomeRNAi; 1915; -.
PMAP-CutDB; P68104; -.
PRO; PR:P68104; -.
Proteomes; UP000005640; Chromosome 6.
Bgee; ENSG00000156508; Expressed in 215 organ(s), highest expression level in right ovary.
CleanEx; HS_EEF1A1; -.
ExpressionAtlas; P68104; baseline and differential.
Genevisible; P68104; HS.
GO; GO:0030864; C:cortical actin cytoskeleton; IDA:UniProtKB.
GO; GO:0005737; C:cytoplasm; IDA:UniProtKB.
GO; GO:0098574; C:cytoplasmic side of lysosomal membrane; NAS:ParkinsonsUK-UCL.
GO; GO:0005829; C:cytosol; IDA:UniProtKB.
GO; GO:0005853; C:eukaryotic translation elongation factor 1 complex; TAS:UniProtKB.
GO; GO:0070062; C:extracellular exosome; HDA:UniProtKB.
GO; GO:0005576; C:extracellular region; TAS:Reactome.
GO; GO:0005615; C:extracellular space; HDA:UniProtKB.
GO; GO:1904813; C:ficolin-1-rich granule lumen; TAS:Reactome.
GO; GO:0016020; C:membrane; HDA:UniProtKB.
GO; GO:0005730; C:nucleolus; IDA:UniProtKB.
GO; GO:0005634; C:nucleus; IDA:UniProtKB.
GO; GO:0005886; C:plasma membrane; IDA:UniProtKB.
GO; GO:0032587; C:ruffle membrane; IDA:UniProtKB.
GO; GO:0034774; C:secretory granule lumen; TAS:Reactome.
GO; GO:0005525; F:GTP binding; TAS:UniProtKB.
GO; GO:0003924; F:GTPase activity; IBA:GO_Central.
GO; GO:0019901; F:protein kinase binding; IPI:UniProtKB.
GO; GO:0003723; F:RNA binding; HDA:UniProtKB.
GO; GO:0003746; F:translation elongation factor activity; IBA:GO_Central.
GO; GO:0000049; F:tRNA binding; IDA:UniProtKB.
GO; GO:0071364; P:cellular response to epidermal growth factor stimulus; IDA:UniProtKB.
GO; GO:0043312; P:neutrophil degranulation; TAS:Reactome.
GO; GO:1904714; P:regulation of chaperone-mediated autophagy; NAS:ParkinsonsUK-UCL.
GO; GO:0006412; P:translation; IBA:GO_Central.
GO; GO:0006414; P:translational elongation; IBA:GO_Central.
HAMAP; MF_00118_A; EF_Tu_A; 1.
InterPro; IPR004161; EFTu-like_2.
InterPro; IPR031157; G_TR_CS.
InterPro; IPR027417; P-loop_NTPase.
InterPro; IPR000795; TF_GTP-bd_dom.
InterPro; IPR009000; Transl_B-barrel_sf.
InterPro; IPR009001; Transl_elong_EF1A/Init_IF2_C.
InterPro; IPR004539; Transl_elong_EF1A_euk/arc.
InterPro; IPR004160; Transl_elong_EFTu/EF1A_C.
Pfam; PF00009; GTP_EFTU; 1.
Pfam; PF03144; GTP_EFTU_D2; 1.
Pfam; PF03143; GTP_EFTU_D3; 1.
PRINTS; PR00315; ELONGATNFCT.
SUPFAM; SSF50447; SSF50447; 1.
SUPFAM; SSF50465; SSF50465; 1.
SUPFAM; SSF52540; SSF52540; 1.
TIGRFAMs; TIGR00483; EF-1_alpha; 1.
PROSITE; PS00301; G_TR_1; 1.
PROSITE; PS51722; G_TR_2; 1.
1: Evidence at protein level;
3D-structure; Acetylation; Alternative splicing; Cell membrane;
Complete proteome; Cytoplasm; Direct protein sequencing;
Elongation factor; GTP-binding; Membrane; Methylation;
Nucleotide-binding; Nucleus; Phosphoprotein; Protein biosynthesis;
Reference proteome; Transcription; Transcription regulation;
Ubl conjugation.
INIT_MET 1 1 Removed. {ECO:0000269|PubMed:26545399}.
CHAIN 2 462 Elongation factor 1-alpha 1.
/FTId=PRO_0000090885.
DOMAIN 5 242 tr-type G.
NP_BIND 14 21 GTP. {ECO:0000250}.
NP_BIND 91 95 GTP. {ECO:0000250}.
NP_BIND 153 156 GTP. {ECO:0000250}.
REGION 14 21 G1. {ECO:0000250}.
REGION 70 74 G2. {ECO:0000250}.
REGION 91 94 G3. {ECO:0000250}.
REGION 153 156 G4. {ECO:0000250}.
REGION 194 196 G5. {ECO:0000250}.
MOD_RES 2 2 N,N,N-trimethylglycine.
{ECO:0000269|PubMed:26545399}.
MOD_RES 36 36 N6,N6,N6-trimethyllysine; alternate; by
EEF1AKMT4. {ECO:0000269|PubMed:28520920}.
MOD_RES 36 36 N6,N6-dimethyllysine; alternate; by
EEF1AKMT4. {ECO:0000269|PubMed:28520920}.
MOD_RES 36 36 N6-methyllysine; alternate; by EEF1AKMT4.
{ECO:0000269|PubMed:28520920}.
MOD_RES 55 55 N6,N6-dimethyllysine.
{ECO:0000269|Ref.7}.
MOD_RES 79 79 N6,N6,N6-trimethyllysine; by EEF1AKMT1.
{ECO:0000269|PubMed:26545399}.
MOD_RES 165 165 N6,N6,N6-trimethyllysine; alternate; by
EEF1AKMT3. {ECO:0000269|PubMed:28108655}.
MOD_RES 165 165 N6,N6-dimethyllysine; alternate; by
EEF1AKMT3. {ECO:0000269|PubMed:28108655,
ECO:0000269|Ref.7}.
MOD_RES 165 165 N6-acetyllysine; alternate.
{ECO:0000250|UniProtKB:P10126}.
MOD_RES 165 165 N6-methyllysine; alternate; by EEF1AKMT3.
{ECO:0000269|PubMed:28108655}.
MOD_RES 172 172 N6-acetyllysine.
{ECO:0000250|UniProtKB:P10126}.
MOD_RES 273 273 N6-acetyllysine.
{ECO:0000250|UniProtKB:P10126}.
MOD_RES 300 300 Phosphoserine; by TGFBR1.
{ECO:0000269|PubMed:20832312}.
MOD_RES 301 301 5-glutamyl
glycerylphosphorylethanolamine.
{ECO:0000269|PubMed:2569467}.
MOD_RES 318 318 N6,N6,N6-trimethyllysine; by EEF1AKMT2.
{ECO:0000269|PubMed:25144183}.
MOD_RES 374 374 5-glutamyl
glycerylphosphorylethanolamine.
{ECO:0000269|PubMed:2569467}.
MOD_RES 392 392 N6-acetyllysine; alternate.
{ECO:0000250|UniProtKB:P10126}.
MOD_RES 392 392 N6-succinyllysine; alternate.
{ECO:0000250|UniProtKB:P10126}.
MOD_RES 432 432 Phosphothreonine; by PASK.
{ECO:0000269|PubMed:17595531}.
MOD_RES 439 439 N6-acetyllysine.
{ECO:0000250|UniProtKB:P10126}.
VAR_SEQ 141 161 Missing (in isoform 2).
{ECO:0000303|PubMed:15489334}.
/FTId=VSP_057184.
MUTAGEN 36 36 K->R: No effect on methylation by
EEF1AKMT2. Abolishes EEF1AKMT4-mediated
methylation.
{ECO:0000269|PubMed:25144183,
ECO:0000269|PubMed:28520920}.
MUTAGEN 55 55 K->R: No effect on methylation by
EEF1AKMT2. {ECO:0000269|PubMed:25144183}.
MUTAGEN 79 79 K->R: No effect on methylation by
EEF1AKMT2. {ECO:0000269|PubMed:25144183}.
MUTAGEN 165 165 K->A: Abolishes methylation by EEF1AKMT3.
{ECO:0000269|PubMed:28108655}.
MUTAGEN 165 165 K->R: No effect on methylation by
EEF1AKMT2. {ECO:0000269|PubMed:25144183}.
MUTAGEN 318 318 K->R: Abolishes methylation by EEF1AKMT2.
{ECO:0000269|PubMed:25144183}.
MUTAGEN 432 432 T->A: Abolishes phosphorylation by PASK.
{ECO:0000269|PubMed:17595531}.
CONFLICT 83 83 S -> A (in Ref. 6; CAA27325).
{ECO:0000305}.
CONFLICT 232 232 L -> V (in Ref. 3; CAA34756).
{ECO:0000305}.
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


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