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 27-MAR-2024, entry version 232. 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="https://atlasgeneticsoncology.org/gene/40408/EEF1A2"; CC --------------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution (CC BY 4.0) License CC --------------------------------------------------------------------------- DR EMBL; 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 PDB; 8B6Z; EM; 2.90 A; A=1-463. DR PDBsum; 3C5J; -. DR PDBsum; 8B6Z; -. DR AlphaFoldDB; Q05639; -. DR EMDB; EMD-15893; -. DR SMR; Q05639; -. DR BioGRID; 108238; 269. DR DIP; DIP-40060N; -. DR IntAct; Q05639; 109. DR MINT; Q05639; -. DR STRING; 9606.ENSP00000217182; -. DR BindingDB; Q05639; -. DR ChEMBL; CHEMBL1795122; -. DR DrugBank; DB04977; Plitidepsin. DR GlyGen; Q05639; 2 sites, 1 O-linked glycan (2 sites). 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; 9606-ENSP00000217182; -. DR PeptideAtlas; Q05639; -. DR PRIDE; Q05639; -. DR ProteomicsDB; 58341; -. DR Pumba; Q05639; -. DR TopDownProteomics; Q05639; -. DR Antibodypedia; 29757; 313 antibodies from 38 providers. DR DNASU; 1917; -. DR Ensembl; ENST00000217182.6; ENSP00000217182.3; ENSG00000101210.14. 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 AGR; HGNC:3192; -. 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; QIRKGYA; -. DR OrthoDB; 5477300at2759; -. 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; 20 hits in 1160 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 169 other cell types or tissues. DR ExpressionAtlas; Q05639; baseline and differential. 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 CDD; cd01883; EF1_alpha; 1. DR CDD; cd03693; EF1_alpha_II; 1. DR CDD; cd03705; EF1_alpha_III; 1. DR Gene3D; 3.40.50.300; P-loop containing nucleotide triphosphate hydrolases; 1. DR Gene3D; 2.40.30.10; Translation factors; 2. 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 NCBIfam; TIGR00483; EF-1_alpha; 1. DR PANTHER; PTHR23115:SF228; ELONGATION FACTOR 1-ALPHA 2; 1. DR PANTHER; PTHR23115; TRANSLATION FACTOR; 1. 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; SSF50465; EF-Tu/eEF-1alpha/eIF2-gamma C-terminal domain; 1. DR SUPFAM; SSF52540; P-loop containing nucleoside triphosphate hydrolases; 1. DR SUPFAM; SSF50447; Translation proteins; 1. DR PROSITE; PS00301; G_TR_1; 1. DR PROSITE; PS51722; G_TR_2; 1. DR Genevisible; Q05639; HS. 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; uncertain significance; dbSNP:rs2082414178)" 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" FT STRAND 7..13 FT /evidence="ECO:0007829|PDB:8B6Z" FT HELIX 20..31 FT /evidence="ECO:0007829|PDB:8B6Z" FT HELIX 36..49 FT /evidence="ECO:0007829|PDB:8B6Z" FT STRAND 50..52 FT /evidence="ECO:0007829|PDB:8B6Z" FT TURN 55..57 FT /evidence="ECO:0007829|PDB:8B6Z" FT HELIX 58..65 FT /evidence="ECO:0007829|PDB:8B6Z" FT STRAND 79..81 FT /evidence="ECO:0007829|PDB:8B6Z" FT STRAND 86..91 FT /evidence="ECO:0007829|PDB:8B6Z" FT STRAND 93..95 FT /evidence="ECO:0007829|PDB:8B6Z" FT HELIX 98..104 FT /evidence="ECO:0007829|PDB:8B6Z" FT STRAND 105..107 FT /evidence="ECO:0007829|PDB:8B6Z" FT STRAND 110..117 FT /evidence="ECO:0007829|PDB:8B6Z" FT HELIX 122..126 FT /evidence="ECO:0007829|PDB:8B6Z" FT HELIX 133..143 FT /evidence="ECO:0007829|PDB:8B6Z" FT STRAND 148..153 FT /evidence="ECO:0007829|PDB:8B6Z" FT HELIX 155..157 FT /evidence="ECO:0007829|PDB:8B6Z" FT STRAND 158..162 FT /evidence="ECO:0007829|PDB:8B6Z" FT HELIX 164..181 FT /evidence="ECO:0007829|PDB:8B6Z" FT HELIX 185..187 FT /evidence="ECO:0007829|PDB:8B6Z" FT STRAND 190..192 FT /evidence="ECO:0007829|PDB:8B6Z" FT TURN 195..200 FT /evidence="ECO:0007829|PDB:8B6Z" FT STRAND 201..203 FT /evidence="ECO:0007829|PDB:8B6Z" FT STRAND 214..216 FT /evidence="ECO:0007829|PDB:8B6Z" FT STRAND 223..227 FT /evidence="ECO:0007829|PDB:8B6Z" FT HELIX 228..233 FT /evidence="ECO:0007829|PDB:8B6Z" FT STRAND 247..249 FT /evidence="ECO:0007829|PDB:8B6Z" FT STRAND 252..256 FT /evidence="ECO:0007829|PDB:8B6Z" FT TURN 257..259 FT /evidence="ECO:0007829|PDB:8B6Z" FT STRAND 260..266 FT /evidence="ECO:0007829|PDB:8B6Z" FT STRAND 277..281 FT /evidence="ECO:0007829|PDB:8B6Z" FT TURN 282..284 FT /evidence="ECO:0007829|PDB:8B6Z" FT STRAND 285..294 FT /evidence="ECO:0007829|PDB:8B6Z" FT STRAND 307..314 FT /evidence="ECO:0007829|PDB:8B6Z" FT TURN 317..319 FT /evidence="ECO:0007829|PDB:8B6Z" FT STRAND 325..328 FT /evidence="ECO:0007829|PDB:8B6Z" FT STRAND 337..346 FT /evidence="ECO:0007829|PDB:8B6Z" FT STRAND 360..363 FT /evidence="ECO:0007829|PDB:8B6Z" FT STRAND 366..379 FT /evidence="ECO:0007829|PDB:8B6Z" FT TURN 381..383 FT /evidence="ECO:0007829|PDB:8B6Z" FT STRAND 386..390 FT /evidence="ECO:0007829|PDB:8B6Z" FT STRAND 399..408 FT /evidence="ECO:0007829|PDB:8B6Z" FT TURN 415..417 FT /evidence="ECO:0007829|PDB:8B6Z" FT HELIX 419..421 FT /evidence="ECO:0007829|PDB:8B6Z" FT STRAND 423..428 FT /evidence="ECO:0007829|PDB:8B6Z" FT STRAND 431..443 FT /evidence="ECO:0007829|PDB:8B6Z" 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 //