EF1A2_HUMAN
ID EF1A2_HUMAN Reviewed; 463 AA.
AC Q05639; B5BUF3; E1P5J1; P54266; Q0VGC7;
DT 01-JUN-1994, integrated into UniProtKB/Swiss-Prot.
DT 01-JUN-1994, sequence version 1.
DT 03-AUG-2022, entry version 223.
DE RecName: Full=Elongation factor 1-alpha 2;
DE Short=EF-1-alpha-2;
DE AltName: Full=Eukaryotic elongation factor 1 A-2;
DE Short=eEF1A-2;
DE AltName: Full=Statin-S1;
GN Name=EEF1A2; Synonyms=EEF1AL, STN;
OS Homo sapiens (Human).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini; Hominidae;
OC Homo.
OX NCBI_TaxID=9606;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA].
RX PubMed=8354261; DOI=10.1111/j.1432-1033.1993.tb18064.x;
RA Knudsen S.M., Frydenberg J., Clark B.F.C., Leffers H.;
RT "Tissue-dependent variation in the expression of elongation factor-1 alpha
RT isoforms: isolation and characterisation of a cDNA encoding a novel variant
RT of human elongation-factor 1 alpha.";
RL Eur. J. Biochem. 215:549-554(1993).
RN [2]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RX PubMed=10950927; DOI=10.1006/geno.2000.6271;
RA Bischoff C., Kahns S., Lund A., Joergensen H.F., Praestegaard M.,
RA Clark B.F.C., Leffers H.;
RT "The human elongation factor 1 A-2 gene (EEF1A2): complete sequence and
RT characterization of gene structure and promoter activity.";
RL Genomics 68:63-70(2000).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RX PubMed=19054851; DOI=10.1038/nmeth.1273;
RA Goshima N., Kawamura Y., Fukumoto A., Miura A., Honma R., Satoh R.,
RA Wakamatsu A., Yamamoto J., Kimura K., Nishikawa T., Andoh T., Iida Y.,
RA Ishikawa K., Ito E., Kagawa N., Kaminaga C., Kanehori K., Kawakami B.,
RA Kenmochi K., Kimura R., Kobayashi M., Kuroita T., Kuwayama H., Maruyama Y.,
RA Matsuo K., Minami K., Mitsubori M., Mori M., Morishita R., Murase A.,
RA Nishikawa A., Nishikawa S., Okamoto T., Sakagami N., Sakamoto Y.,
RA Sasaki Y., Seki T., Sono S., Sugiyama A., Sumiya T., Takayama T.,
RA Takayama Y., Takeda H., Togashi T., Yahata K., Yamada H., Yanagisawa Y.,
RA Endo Y., Imamoto F., Kisu Y., Tanaka S., Isogai T., Imai J., Watanabe S.,
RA Nomura N.;
RT "Human protein factory for converting the transcriptome into an in vitro-
RT expressed proteome.";
RL Nat. Methods 5:1011-1017(2008).
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=11780052; DOI=10.1038/414865a;
RA Deloukas P., Matthews L.H., Ashurst J.L., Burton J., Gilbert J.G.R.,
RA Jones M., Stavrides G., Almeida J.P., Babbage A.K., Bagguley C.L.,
RA Bailey J., Barlow K.F., Bates K.N., Beard L.M., Beare D.M., Beasley O.P.,
RA Bird C.P., Blakey S.E., Bridgeman A.M., Brown A.J., Buck D., Burrill W.D.,
RA Butler A.P., Carder C., Carter N.P., Chapman J.C., Clamp M., Clark G.,
RA Clark L.N., Clark S.Y., Clee C.M., Clegg S., Cobley V.E., Collier R.E.,
RA Connor R.E., Corby N.R., Coulson A., Coville G.J., Deadman R., Dhami P.D.,
RA Dunn M., Ellington A.G., Frankland J.A., Fraser A., French L., Garner P.,
RA Grafham D.V., Griffiths C., Griffiths M.N.D., Gwilliam R., Hall R.E.,
RA Hammond S., Harley J.L., Heath P.D., Ho S., Holden J.L., Howden P.J.,
RA Huckle E., Hunt A.R., Hunt S.E., Jekosch K., Johnson C.M., Johnson D.,
RA Kay M.P., Kimberley A.M., King A., Knights A., Laird G.K., Lawlor S.,
RA Lehvaeslaiho M.H., Leversha M.A., Lloyd C., Lloyd D.M., Lovell J.D.,
RA Marsh V.L., Martin S.L., McConnachie L.J., McLay K., McMurray A.A.,
RA Milne S.A., Mistry D., Moore M.J.F., Mullikin J.C., Nickerson T.,
RA Oliver K., Parker A., Patel R., Pearce T.A.V., Peck A.I.,
RA Phillimore B.J.C.T., Prathalingam S.R., Plumb R.W., Ramsay H., Rice C.M.,
RA Ross M.T., Scott C.E., Sehra H.K., Shownkeen R., Sims S., Skuce C.D.,
RA Smith M.L., Soderlund C., Steward C.A., Sulston J.E., Swann R.M.,
RA Sycamore N., Taylor R., Tee L., Thomas D.W., Thorpe A., Tracey A.,
RA Tromans A.C., Vaudin M., Wall M., Wallis J.M., Whitehead S.L.,
RA Whittaker P., Willey D.L., Williams L., Williams S.A., Wilming L.,
RA Wray P.W., Hubbard T., Durbin R.M., Bentley D.R., Beck S., Rogers J.;
RT "The DNA sequence and comparative analysis of human chromosome 20.";
RL Nature 414:865-871(2001).
RN [5]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RA Mural R.J., Istrail S., Sutton G.G., Florea L., Halpern A.L., Mobarry C.M.,
RA Lippert R., Walenz B., Shatkay H., Dew I., Miller J.R., Flanigan M.J.,
RA Edwards N.J., Bolanos R., Fasulo D., Halldorsson B.V., Hannenhalli S.,
RA Turner R., Yooseph S., Lu F., Nusskern D.R., Shue B.C., Zheng X.H.,
RA Zhong F., Delcher A.L., Huson D.H., Kravitz S.A., Mouchard L., Reinert K.,
RA Remington K.A., Clark A.G., Waterman M.S., Eichler E.E., Adams M.D.,
RA Hunkapiller M.W., Myers E.W., Venter J.C.;
RL Submitted (SEP-2005) to the EMBL/GenBank/DDBJ databases.
RN [6]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC TISSUE=Duodenum, and Lung;
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 project:
RT the Mammalian Gene Collection (MGC).";
RL Genome Res. 14:2121-2127(2004).
RN [7]
RP NUCLEOTIDE SEQUENCE [MRNA] OF 29-463.
RC TISSUE=Hippocampus;
RX PubMed=7945283; DOI=10.1006/bbrc.1994.2336;
RA Lee S., Ann D.K., Wang E.;
RT "Cloning of human and mouse brain cDNAs coding for S1, the second member of
RT the mammalian elongation factor-1 alpha gene family: analysis of a possible
RT evolutionary pathway.";
RL Biochem. Biophys. Res. Commun. 203:1371-1377(1994).
RN [8]
RP ACETYLATION [LARGE SCALE ANALYSIS] AT LYS-179 AND LYS-439, AND
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=19608861; DOI=10.1126/science.1175371;
RA Choudhary C., Kumar C., Gnad F., Nielsen M.L., Rehman M., Walther T.C.,
RA Olsen J.V., Mann M.;
RT "Lysine acetylation targets protein complexes and co-regulates major
RT cellular functions.";
RL Science 325:834-840(2009).
RN [9]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=21269460; DOI=10.1186/1752-0509-5-17;
RA Burkard T.R., Planyavsky M., Kaupe I., Breitwieser F.P., Buerckstuemmer T.,
RA Bennett K.L., Superti-Furga G., Colinge J.;
RT "Initial characterization of the human central proteome.";
RL BMC Syst. Biol. 5:17-17(2011).
RN [10]
RP METHYLATION [LARGE SCALE ANALYSIS] AT LYS-79 AND LYS-165, AND
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Colon carcinoma;
RX PubMed=24129315; DOI=10.1074/mcp.o113.027870;
RA Guo A., Gu H., Zhou J., Mulhern D., Wang Y., Lee K.A., Yang V., Aguiar M.,
RA Kornhauser J., Jia X., Ren J., Beausoleil S.A., Silva J.C., Vemulapalli V.,
RA Bedford M.T., Comb M.J.;
RT "Immunoaffinity enrichment and mass spectrometry analysis of protein
RT methylation.";
RL Mol. Cell. Proteomics 13:372-387(2014).
RN [11]
RP METHYLATION AT LYS-165, AND MUTAGENESIS OF LYS-165.
RX PubMed=28108655; DOI=10.1093/nar/gkx002;
RA Malecki J., Aileni V.K., Ho A.Y., Schwarz J., Moen A., Soerensen V.,
RA Nilges B.S., Jakobsson M.E., Leidel S.A., Falnes P.O.;
RT "The novel lysine specific methyltransferase METTL21B affects mRNA
RT translation through inducible and dynamic methylation of Lys-165 in human
RT eukaryotic elongation factor 1 alpha (eEF1A).";
RL Nucleic Acids Res. 45:4370-4389(2017).
RN [12]
RP METHYLATION AT LYS-36, IDENTIFICATION BY MASS SPECTROMETRY, AND MUTAGENESIS
RP OF LYS-36.
RX PubMed=28520920; DOI=10.1093/nar/gkx432;
RA Jakobsson M.E., Malecki J., Nilges B.S., Moen A., Leidel S.A., Falnes P.O.;
RT "Methylation of human eukaryotic elongation factor alpha (eEF1A) by a
RT member of a novel protein lysine methyltransferase family modulates mRNA
RT translation.";
RL Nucleic Acids Res. 45:8239-8254(2017).
RN [13]
RP METHYLATION AT LYS-55 BY METTL13.
RX PubMed=30612740; DOI=10.1016/j.cell.2018.11.038;
RA Liu S., Hausmann S., Carlson S.M., Fuentes M.E., Francis J.W., Pillai R.,
RA Lofgren S.M., Hulea L., Tandoc K., Lu J., Li A., Nguyen N.D., Caporicci M.,
RA Kim M.P., Maitra A., Wang H., Wistuba I.I., Porco J.A. Jr., Bassik M.C.,
RA Elias J.E., Song J., Topisirovic I., Van Rechem C., Mazur P.K., Gozani O.;
RT "METTL13 methylation of eEF1A increases translational output to promote
RT tumorigenesis.";
RL Cell 0:0-0(2018).
RN [14]
RP METHYLATION AT N-TERMINUS AND AT LYS-55 BY METTL13.
RX PubMed=30143613; DOI=10.1038/s41467-018-05646-y;
RA Jakobsson M.E., Malecki J.M., Halabelian L., Nilges B.S., Pinto R.,
RA Kudithipudi S., Munk S., Davydova E., Zuhairi F.R., Arrowsmith C.H.,
RA Jeltsch A., Leidel S.A., Olsen J.V., Falnes P.O.;
RT "The dual methyltransferase METTL13 targets N terminus and Lys55 of eEF1A
RT and modulates codon-specific translation rates.";
RL Nat. Commun. 9:3411-3411(2018).
RN [15]
RP X-RAY CRYSTALLOGRAPHY (1.8 ANGSTROMS) OF 343-355 IN COMPLEX WITH
RP HLA-DRA/HLA-DRB3 HETERODIMER.
RX PubMed=18697946; DOI=10.1073/pnas.0805810105;
RA Dai S., Crawford F., Marrack P., Kappler J.W.;
RT "The structure of HLA-DR52c: comparison to other HLA-DRB3 alleles.";
RL Proc. Natl. Acad. Sci. U.S.A. 105:11893-11897(2008).
RN [16]
RP INVOLVEMENT IN DEE33, AND VARIANT DEE33 SER-70.
RX PubMed=23033978; DOI=10.1056/nejmoa1206524;
RA de Ligt J., Willemsen M.H., van Bon B.W., Kleefstra T., Yntema H.G.,
RA Kroes T., Vulto-van Silfhout A.T., Koolen D.A., de Vries P., Gilissen C.,
RA del Rosario M., Hoischen A., Scheffer H., de Vries B.B., Brunner H.G.,
RA Veltman J.A., Vissers L.E.;
RT "Diagnostic exome sequencing in persons with severe intellectual
RT disability.";
RL N. Engl. J. Med. 367:1921-1929(2012).
RN [17]
RP INVOLVEMENT IN DEE33, AND VARIANT DEE33 SER-70.
RX PubMed=23647072; DOI=10.1111/epi.12201;
RA Veeramah K.R., Johnstone L., Karafet T.M., Wolf D., Sprissler R.,
RA Salogiannis J., Barth-Maron A., Greenberg M.E., Stuhlmann T., Weinert S.,
RA Jentsch T.J., Pazzi M., Restifo L.L., Talwar D., Erickson R.P.,
RA Hammer M.F.;
RT "Exome sequencing reveals new causal mutations in children with epileptic
RT encephalopathies.";
RL Epilepsia 54:1270-1281(2013).
RN [18]
RP INVOLVEMENT IN MRD38, AND VARIANTS MRD38 LYS-122 AND HIS-252.
RX PubMed=24697219; DOI=10.1111/cge.12394;
RA Nakajima J., Okamoto N., Tohyama J., Kato M., Arai H., Funahashi O.,
RA Tsurusaki Y., Nakashima M., Kawashima H., Saitsu H., Matsumoto N.,
RA Miyake N.;
RT "De novo EEF1A2 mutations in patients with characteristic facial features,
RT intellectual disability, autistic behaviors and epilepsy.";
RL Clin. Genet. 87:356-361(2015).
RN [19]
RP VARIANT THR-92.
RX PubMed=26740508; DOI=10.1136/jmedgenet-2015-103568;
RA Lopes F., Barbosa M., Ameur A., Soares G., de Sa J., Dias A.I.,
RA Oliveira G., Cabral P., Temudo T., Calado E., Cruz I.F., Vieira J.P.,
RA Oliveira R., Esteves S., Sauer S., Jonasson I., Syvaenen A.C.,
RA Gyllensten U., Pinto D., Maciel P.;
RT "Identification of novel genetic causes of Rett syndrome-like phenotypes.";
RL J. Med. Genet. 53:190-199(2016).
CC -!- FUNCTION: This protein promotes the GTP-dependent binding of aminoacyl-
CC tRNA to the A-site of ribosomes during protein biosynthesis.
CC -!- SUBUNIT: Monomer. {ECO:0000250}.
CC -!- INTERACTION:
CC Q05639; Q969K4: ABTB1; NbExp=9; IntAct=EBI-354943, EBI-7223971;
CC Q05639; P42858: HTT; NbExp=3; IntAct=EBI-354943, EBI-466029;
CC Q05639; Q5S007: LRRK2; NbExp=3; IntAct=EBI-354943, EBI-5323863;
CC Q05639; Q14166: TTLL12; NbExp=4; IntAct=EBI-354943, EBI-923010;
CC Q05639; P59595: N; Xeno; NbExp=10; IntAct=EBI-354943, EBI-7602718;
CC -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000250}.
CC -!- TISSUE SPECIFICITY: Brain, heart, and skeletal muscle.
CC -!- PTM: Trimethylated at Lys-165 by EEF1AKMT3 (PubMed:28108655). Mono-,
CC di-, and trimethylated at Lys-36 by EEF1AKMT4; trimethylated form is
CC predominant. Methylation by EEF1AKMT4 contributes to the fine-tuning of
CC translation rates for a subset of tRNAs (PubMed:28520920).
CC Trimethylated at the N-terminus by METTL13 (PubMed:30143613). Mono- and
CC dimethylated at Lys-55 by METTL13; dimethylated form is predominant
CC (PubMed:30143613, PubMed:30612740). {ECO:0000269|PubMed:28108655,
CC ECO:0000269|PubMed:28520920, ECO:0000269|PubMed:30143613,
CC ECO:0000269|PubMed:30612740}.
CC -!- DISEASE: Developmental and epileptic encephalopathy 33 (DEE33)
CC [MIM:616409]: A form of epileptic encephalopathy, a heterogeneous group
CC of severe early-onset epilepsies characterized by refractory seizures,
CC neurodevelopmental impairment, and poor prognosis. Development is
CC normal prior to seizure onset, after which cognitive and motor delays
CC become apparent. {ECO:0000269|PubMed:23033978,
CC ECO:0000269|PubMed:23647072}. Note=The disease is caused by variants
CC affecting the gene represented in this entry.
CC -!- DISEASE: Intellectual developmental disorder, autosomal dominant 38
CC (MRD38) [MIM:616393]: A disorder characterized by significantly below
CC average general intellectual functioning associated with impairments in
CC adaptive behavior and manifested during the developmental period. MRD38
CC common features are severe intellectual disability, autistic behavior,
CC absent speech, neonatal hypotonia, epilepsy and progressive
CC microcephaly. {ECO:0000269|PubMed:24697219}. Note=The disease is caused
CC by variants affecting the gene represented in this entry.
CC -!- SIMILARITY: Belongs to the TRAFAC class translation factor GTPase
CC superfamily. Classic translation factor GTPase family. EF-Tu/EF-1A
CC subfamily. {ECO:0000305}.
CC -!- WEB RESOURCE: Name=Atlas of Genetics and Cytogenetics in Oncology and
CC Haematology;
CC URL="http://atlasgeneticsoncology.org/Genes/EEF1A2ID40408ch20q13.html";
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DR EMBL; X70940; CAA50280.1; -; mRNA.
DR EMBL; AF163763; AAF80488.1; -; Genomic_DNA.
DR EMBL; AB451389; BAG70203.1; -; mRNA.
DR EMBL; AL121829; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; CH471077; EAW75260.1; -; Genomic_DNA.
DR EMBL; BC000432; AAH00432.1; -; mRNA.
DR EMBL; BC110409; AAI10410.1; -; mRNA.
DR EMBL; L10340; AAA91835.1; -; mRNA.
DR CCDS; CCDS13522.1; -.
DR PIR; S35033; EFHUA2.
DR RefSeq; NP_001949.1; NM_001958.3.
DR PDB; 3C5J; X-ray; 1.80 A; C=343-355.
DR PDBsum; 3C5J; -.
DR AlphaFoldDB; Q05639; -.
DR SMR; Q05639; -.
DR BioGRID; 108238; 241.
DR DIP; DIP-40060N; -.
DR IntAct; Q05639; 105.
DR MINT; Q05639; -.
DR STRING; 9606.ENSP00000217182; -.
DR BindingDB; Q05639; -.
DR ChEMBL; CHEMBL1795122; -.
DR GlyGen; Q05639; 1 site, 1 O-linked glycan (1 site).
DR iPTMnet; Q05639; -.
DR MetOSite; Q05639; -.
DR PhosphoSitePlus; Q05639; -.
DR SwissPalm; Q05639; -.
DR BioMuta; EEF1A2; -.
DR DMDM; 544231; -.
DR EPD; Q05639; -.
DR jPOST; Q05639; -.
DR MassIVE; Q05639; -.
DR MaxQB; Q05639; -.
DR PaxDb; Q05639; -.
DR PeptideAtlas; Q05639; -.
DR PRIDE; Q05639; -.
DR ProteomicsDB; 58341; -.
DR TopDownProteomics; Q05639; -.
DR Antibodypedia; 29757; 258 antibodies from 38 providers.
DR DNASU; 1917; -.
DR Ensembl; ENST00000217182.6; ENSP00000217182.3; ENSG00000101210.13.
DR GeneID; 1917; -.
DR KEGG; hsa:1917; -.
DR MANE-Select; ENST00000217182.6; ENSP00000217182.3; NM_001958.5; NP_001949.1.
DR UCSC; uc002yfe.3; human.
DR CTD; 1917; -.
DR DisGeNET; 1917; -.
DR GeneCards; EEF1A2; -.
DR HGNC; HGNC:3192; EEF1A2.
DR HPA; ENSG00000101210; Tissue enriched (skeletal).
DR MalaCards; EEF1A2; -.
DR MIM; 602959; gene.
DR MIM; 616393; phenotype.
DR MIM; 616409; phenotype.
DR neXtProt; NX_Q05639; -.
DR OpenTargets; ENSG00000101210; -.
DR Orphanet; 178469; Autosomal dominant non-syndromic intellectual disability.
DR Orphanet; 442835; Non-specific early-onset epileptic encephalopathy.
DR PharmGKB; PA36219; -.
DR VEuPathDB; HostDB:ENSG00000101210; -.
DR eggNOG; KOG0052; Eukaryota.
DR GeneTree; ENSGT00950000183029; -.
DR HOGENOM; CLU_007265_3_5_1; -.
DR InParanoid; Q05639; -.
DR OMA; VACTFES; -.
DR OrthoDB; 1150082at2759; -.
DR PhylomeDB; Q05639; -.
DR TreeFam; TF300304; -.
DR PathwayCommons; Q05639; -.
DR Reactome; R-HSA-156842; Eukaryotic Translation Elongation.
DR SignaLink; Q05639; -.
DR SIGNOR; Q05639; -.
DR BioGRID-ORCS; 1917; 16 hits in 1082 CRISPR screens.
DR ChiTaRS; EEF1A2; human.
DR EvolutionaryTrace; Q05639; -.
DR GeneWiki; EEF1A2; -.
DR GenomeRNAi; 1917; -.
DR Pharos; Q05639; Tchem.
DR PRO; PR:Q05639; -.
DR Proteomes; UP000005640; Chromosome 20.
DR RNAct; Q05639; protein.
DR Bgee; ENSG00000101210; Expressed in gastrocnemius and 167 other tissues.
DR ExpressionAtlas; Q05639; baseline and differential.
DR Genevisible; Q05639; HS.
DR GO; GO:0005737; C:cytoplasm; IDA:UniProtKB.
DR GO; GO:0098574; C:cytoplasmic side of lysosomal membrane; NAS:ParkinsonsUK-UCL.
DR GO; GO:0005853; C:eukaryotic translation elongation factor 1 complex; IEA:Ensembl.
DR GO; GO:0045202; C:synapse; IEA:Ensembl.
DR GO; GO:0005525; F:GTP binding; IEA:UniProtKB-KW.
DR GO; GO:0003924; F:GTPase activity; IBA:GO_Central.
DR GO; GO:0019901; F:protein kinase binding; IPI:UniProtKB.
DR GO; GO:0003746; F:translation elongation factor activity; IBA:GO_Central.
DR GO; GO:0008135; F:translation factor activity, RNA binding; NAS:ProtInc.
DR GO; GO:0043065; P:positive regulation of apoptotic process; IEA:Ensembl.
DR GO; GO:0090218; P:positive regulation of lipid kinase activity; IDA:UniProtKB.
DR GO; GO:1904714; P:regulation of chaperone-mediated autophagy; NAS:ParkinsonsUK-UCL.
DR GO; GO:0006412; P:translation; IBA:GO_Central.
DR GO; GO:0006414; P:translational elongation; IBA:GO_Central.
DR Gene3D; 3.40.50.300; -; 1.
DR HAMAP; MF_00118_A; EF_Tu_A; 1.
DR IDEAL; IID00166; -.
DR InterPro; IPR004161; EFTu-like_2.
DR InterPro; IPR031157; G_TR_CS.
DR InterPro; IPR027417; P-loop_NTPase.
DR InterPro; IPR000795; T_Tr_GTP-bd_dom.
DR InterPro; IPR009000; Transl_B-barrel_sf.
DR InterPro; IPR009001; Transl_elong_EF1A/Init_IF2_C.
DR InterPro; IPR004539; Transl_elong_EF1A_euk/arc.
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; G_TR_1; 1.
DR PROSITE; PS51722; G_TR_2; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Acetylation; Autism spectrum disorder; Disease variant;
KW Elongation factor; Epilepsy; GTP-binding; Intellectual disability;
KW Methylation; Nucleotide-binding; Nucleus; Phosphoprotein;
KW Protein biosynthesis; Reference proteome.
FT INIT_MET 1
FT /note="Removed"
FT /evidence="ECO:0000250|UniProtKB:P62631"
FT CHAIN 2..463
FT /note="Elongation factor 1-alpha 2"
FT /id="PRO_0000090891"
FT DOMAIN 5..242
FT /note="tr-type G"
FT REGION 14..21
FT /note="G1"
FT /evidence="ECO:0000250"
FT REGION 70..74
FT /note="G2"
FT /evidence="ECO:0000250"
FT REGION 91..94
FT /note="G3"
FT /evidence="ECO:0000250"
FT REGION 153..156
FT /note="G4"
FT /evidence="ECO:0000250"
FT REGION 194..196
FT /note="G5"
FT /evidence="ECO:0000250"
FT REGION 444..463
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 14..21
FT /ligand="GTP"
FT /ligand_id="ChEBI:CHEBI:37565"
FT /evidence="ECO:0000250"
FT BINDING 91..95
FT /ligand="GTP"
FT /ligand_id="ChEBI:CHEBI:37565"
FT /evidence="ECO:0000250"
FT BINDING 153..156
FT /ligand="GTP"
FT /ligand_id="ChEBI:CHEBI:37565"
FT /evidence="ECO:0000250"
FT MOD_RES 2
FT /note="N,N,N-trimethylglycine"
FT /evidence="ECO:0000250|UniProtKB:P68104"
FT MOD_RES 36
FT /note="N6,N6,N6-trimethyllysine; alternate; by EEF1AKMT4"
FT /evidence="ECO:0000269|PubMed:28520920"
FT MOD_RES 36
FT /note="N6,N6-dimethyllysine; alternate; by EEF1AKMT4"
FT /evidence="ECO:0000269|PubMed:28520920"
FT MOD_RES 36
FT /note="N6-methyllysine; alternate; by EEF1AKMT4"
FT /evidence="ECO:0000269|PubMed:28520920"
FT MOD_RES 55
FT /note="N6,N6,N6-trimethyllysine"
FT /evidence="ECO:0000250|UniProtKB:Q71V39"
FT MOD_RES 55
FT /note="N6,N6-dimethyllysine"
FT /evidence="ECO:0000269|PubMed:30143613,
FT ECO:0000269|PubMed:30612740"
FT MOD_RES 79
FT /note="N6,N6,N6-trimethyllysine"
FT /evidence="ECO:0007744|PubMed:24129315"
FT MOD_RES 165
FT /note="N6,N6,N6-trimethyllysine; alternate; by EEF1AKMT3"
FT /evidence="ECO:0000269|PubMed:28108655"
FT MOD_RES 165
FT /note="N6,N6-dimethyllysine; alternate"
FT /evidence="ECO:0007744|PubMed:24129315"
FT MOD_RES 165
FT /note="N6-methyllysine; alternate"
FT /evidence="ECO:0007744|PubMed:24129315"
FT MOD_RES 179
FT /note="N6-acetyllysine"
FT /evidence="ECO:0007744|PubMed:19608861"
FT MOD_RES 224
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:P62632"
FT MOD_RES 301
FT /note="5-glutamyl glycerylphosphorylethanolamine"
FT /evidence="ECO:0000250|UniProtKB:Q71V39"
FT MOD_RES 374
FT /note="5-glutamyl glycerylphosphorylethanolamine"
FT /evidence="ECO:0000250|UniProtKB:Q71V39"
FT MOD_RES 439
FT /note="N6-acetyllysine"
FT /evidence="ECO:0007744|PubMed:19608861"
FT VARIANT 70
FT /note="G -> S (in DEE33; dbSNP:rs587777162)"
FT /evidence="ECO:0000269|PubMed:23033978,
FT ECO:0000269|PubMed:23647072"
FT /id="VAR_069395"
FT VARIANT 92
FT /note="A -> T (found in a patient with Rett syndrome-like
FT phenotype; unknown pathological significance)"
FT /evidence="ECO:0000269|PubMed:26740508"
FT /id="VAR_079033"
FT VARIANT 122
FT /note="E -> K (in MRD38; dbSNP:rs786205866)"
FT /evidence="ECO:0000269|PubMed:24697219"
FT /id="VAR_073807"
FT VARIANT 252
FT /note="D -> H (in MRD38; dbSNP:rs786205865)"
FT /evidence="ECO:0000269|PubMed:24697219"
FT /id="VAR_073808"
FT MUTAGEN 36
FT /note="K->R: Abolishes EEF1AKMT4-mediated methylation."
FT /evidence="ECO:0000269|PubMed:28520920"
FT MUTAGEN 165
FT /note="K->A: Abolishes methylation by EEF1AKMT3."
FT /evidence="ECO:0000269|PubMed:28108655"
FT CONFLICT 427
FT /note="R -> P (in Ref. 7; AAA91835)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 463 AA; 50470 MW; 31E4E341CEE797EC CRC64;
MGKEKTHINI VVIGHVDSGK STTTGHLIYK CGGIDKRTIE KFEKEAAEMG KGSFKYAWVL
DKLKAERERG ITIDISLWKF ETTKYYITII DAPGHRDFIK NMITGTSQAD CAVLIVAAGV
GEFEAGISKN GQTREHALLA YTLGVKQLIV GVNKMDSTEP AYSEKRYDEI VKEVSAYIKK
IGYNPATVPF VPISGWHGDN MLEPSPNMPW FKGWKVERKE GNASGVSLLE ALDTILPPTR
PTDKPLRLPL QDVYKIGGIG TVPVGRVETG ILRPGMVVTF APVNITTEVK SVEMHHEALS
EALPGDNVGF NVKNVSVKDI RRGNVCGDSK SDPPQEAAQF TSQVIILNHP GQISAGYSPV
IDCHTAHIAC KFAELKEKID RRSGKKLEDN PKSLKSGDAA IVEMVPGKPM CVESFSQYPP
LGRFAVRDMR QTVAVGVIKN VEKKSGGAGK VTKSAQKAQK AGK
