ID EF1A1_HUMAN Reviewed; 462 AA. AC P68104; P04719; P04720; Q6IQ15; DT 13-AUG-1987, integrated into UniProtKB/Swiss-Prot. DT 13-AUG-1987, sequence version 1. DT 11-NOV-2015, entry version 144. 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] (ISOFORM 1). 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] (ISOFORM 1). 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] (ISOFORM 1). 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] (ISOFORMS 1 AND 2). RC TISSUE=B-cell, Bone marrow, Cervix, Colon, Hippocampus, Kidney, Lung, RC Lymph, 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 (ISOFORM 1/2). 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 RP IDENTIFICATION BY MASS 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 (ISOFORM 1). 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 INTERACTION WITH ZPR1, AND SUBCELLULAR LOCATION. RX PubMed=8650580; DOI=10.1126/science.272.5269.1797; RA Galcheva-Gargova Z., Konstantinov K.N., Wu I.-H., Klier F.G., RA Barrett T., Davis R.J.; RT "Binding of zinc finger protein ZPR1 to the epidermal growth factor RT receptor."; RL Science 272:1797-1802(1996). RN [13] 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 [14] 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 [15] 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 [16] 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 [17] 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 [18] 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 [19] 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 [20] 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 [21] 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 {ECO:0000269|PubMed:17177976}. 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. Interacts with ZPR1; the interaction occurs in a CC epidermal growth factor (EGF)-dependent manner. {ECO:0000250, CC ECO:0000269|PubMed:12426392, ECO:0000269|PubMed:12426393, CC ECO:0000269|PubMed:17177976, ECO:0000269|PubMed:17980171, CC ECO:0000269|PubMed:18029264, ECO:0000269|PubMed:19158340, CC ECO:0000269|PubMed:8650580}. 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 Q8IUH5:ZDHHC17; NbExp=2; IntAct=EBI-352162, EBI-524753; CC -!- SUBCELLULAR LOCATION: Cytoplasm. Nucleus. Nucleus, nucleolus. CC Note=Colocalizes with DLC1 at actin-rich regions in the cell CC periphery. Translocates together with ZPR1 from the cytoplasm to CC the nucleus and nucleolus after treatment with mitogens. CC -!- ALTERNATIVE PRODUCTS: CC Event=Alternative splicing; Named isoforms=2; CC Name=1; CC IsoId=P68104-1; Sequence=Displayed; CC Name=2; CC IsoId=P68104-2; Sequence=VSP_057184; CC Note=No experimental confirmation available.; 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. {ECO:0000269|PubMed:9677419}. CC -!- PTM: ISGylated. {ECO:0000269|PubMed:16139798}. CC -!- PTM: Phosphorylated by TXK. Phosphorylation by PASK increases CC translation efficiency. {ECO:0000269|PubMed:17177976, CC ECO:0000269|PubMed:17595531, ECO:0000269|PubMed:20832312}. 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 -!- SIMILARITY: Contains 1 tr-type G (guanine nucleotide-binding) CC domain. {ECO:0000305}. CC -!- SEQUENCE CAUTION: CC Sequence=AAA52367.1; Type=Erroneous initiation; Evidence={ECO:0000305}; CC -!- WEB RESOURCE: Name=Atlas of Genetics and Cytogenetics in Oncology CC and Haematology; CC URL="http://atlasgeneticsoncology.org/Genes/EEF1A1ID40407ch6q13.html"; 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; 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; BC071619; AAH71619.1; -; 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 CCDS; CCDS4980.1; -. [P68104-1] DR PIR; B24977; EFHU1. DR RefSeq; NP_001393.1; NM_001402.5. [P68104-1] DR RefSeq; XP_011533816.1; XM_011535514.1. [P68104-1] DR UniGene; Hs.535192; -. DR UniGene; Hs.586423; -. DR UniGene; Hs.745122; -. DR PDB; 1SYW; Model; -; A=2-443. DR PDB; 3C5J; X-ray; 1.80 A; C=343-355. DR PDBsum; 1SYW; -. DR PDBsum; 3C5J; -. DR ProteinModelPortal; P68104; -. DR SMR; P68104; 4-455. DR BioGrid; 108237; 316. DR DIP; DIP-31277N; -. DR IntAct; P68104; 173. DR MINT; MINT-1180846; -. DR STRING; 9606.ENSP00000330054; -. DR BindingDB; P68104; -. DR ChEMBL; CHEMBL1795120; -. DR PhosphoSite; P68104; -. DR BioMuta; EEF1A1; -. DR DMDM; 55584035; -. DR OGP; P68104; -. DR SWISS-2DPAGE; P68104; -. DR UCD-2DPAGE; P68104; -. DR MaxQB; P68104; -. DR PaxDb; P68104; -. DR PRIDE; P68104; -. DR DNASU; 1915; -. DR Ensembl; ENST00000309268; ENSP00000339053; ENSG00000156508. [P68104-1] DR Ensembl; ENST00000316292; ENSP00000339063; ENSG00000156508. [P68104-1] DR Ensembl; ENST00000331523; ENSP00000330054; ENSG00000156508. [P68104-1] DR GeneID; 1915; -. DR KEGG; hsa:1915; -. DR UCSC; uc003phi.3; human. [P68104-1] DR CTD; 1915; -. DR GeneCards; EEF1A1; -. DR H-InvDB; HIX0020005; -. DR H-InvDB; HIX0032108; -. DR H-InvDB; HIX0033669; -. DR H-InvDB; HIX0169110; -. DR HGNC; HGNC:3189; EEF1A1. DR HPA; HPA051759; -. DR HPA; HPA053862; -. DR HPA; HPA056990; -. DR MIM; 130590; gene. DR neXtProt; NX_P68104; -. DR PharmGKB; PA27625; -. DR eggNOG; KOG0052; Eukaryota. DR eggNOG; COG5256; LUCA. DR HOGENOM; HOG000229291; -. DR HOVERGEN; HBG000179; -. DR InParanoid; P68104; -. DR KO; K03231; -. DR OMA; PASTIFH; -. DR OrthoDB; EOG7NKKK3; -. DR PhylomeDB; P68104; -. DR TreeFam; TF300304; -. DR Reactome; R-HSA-156842; Eukaryotic Translation Elongation. DR Reactome; R-HSA-156902; Peptide chain elongation. DR Reactome; R-HSA-3371511; HSF1 activation. 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 Proteomes; UP000005640; Chromosome 6. DR Bgee; P68104; -. DR CleanEx; HS_EEF1A1; -. DR ExpressionAtlas; P68104; baseline and differential. DR Genevisible; P68104; HS. DR GO; GO:0030864; C:cortical actin cytoskeleton; IDA:UniProtKB. DR GO; GO:0005737; C:cytoplasm; IDA:UniProtKB. DR GO; GO:0005829; C:cytosol; IDA:UniProtKB. DR GO; GO:0005853; C:eukaryotic translation elongation factor 1 complex; TAS:UniProtKB. DR GO; GO:0070062; C:extracellular exosome; IDA:UniProtKB. DR GO; GO:0005615; C:extracellular space; IDA:UniProtKB. DR GO; GO:0016020; C:membrane; IDA:UniProtKB. DR GO; GO:0043209; C:myelin sheath; IEA:Ensembl. DR GO; GO:0005730; C:nucleolus; IDA:UniProtKB. DR GO; GO:0005634; C:nucleus; IDA:UniProtKB. DR GO; GO:0032587; C:ruffle membrane; IDA:UniProtKB. DR GO; GO:0005525; F:GTP binding; TAS:UniProtKB. DR GO; GO:0003924; F:GTPase activity; IBA:GO_Central. DR GO; GO:0044822; F:poly(A) RNA binding; IDA:UniProtKB. DR GO; GO:0019901; F:protein kinase binding; IPI:UniProtKB. DR GO; GO:0003746; F:translation elongation factor activity; TAS:UniProtKB. DR GO; GO:0000049; F:tRNA binding; IDA:UniProtKB. DR GO; GO:0044267; P:cellular protein metabolic process; TAS:Reactome. DR GO; GO:0071364; P:cellular response to epidermal growth factor stimulus; IDA:UniProtKB. DR GO; GO:0010467; P:gene expression; TAS:Reactome. DR GO; GO:0006355; P:regulation of transcription, DNA-templated; IEA:UniProtKB-KW. DR GO; GO:0006351; P:transcription, DNA-templated; IEA:UniProtKB-KW. DR GO; GO:0006412; P:translation; TAS:Reactome. DR GO; GO:0006414; P:translational elongation; TAS:UniProtKB. DR Gene3D; 3.40.50.300; -; 1. DR HAMAP; MF_00118_A; EF_Tu_A; 1. DR InterPro; IPR031157; G_TR_CS. DR InterPro; IPR027417; P-loop_NTPase. DR InterPro; IPR000795; TF_GTP-bd_dom. 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; 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; Alternative splicing; Complete proteome; KW Cytoplasm; Direct protein sequencing; Elongation factor; GTP-binding; KW Methylation; Nucleotide-binding; Nucleus; Phosphoprotein; KW Protein biosynthesis; Reference proteome; Transcription; KW Transcription regulation; Ubl conjugation. FT CHAIN 1 462 Elongation factor 1-alpha 1. FT /FTId=PRO_0000090885. FT DOMAIN 5 242 tr-type G. FT NP_BIND 14 21 GTP. {ECO:0000250}. FT NP_BIND 91 95 GTP. {ECO:0000250}. FT NP_BIND 153 156 GTP. {ECO:0000250}. FT REGION 14 21 G1. {ECO:0000250}. FT REGION 70 74 G2. {ECO:0000250}. FT REGION 91 94 G3. {ECO:0000250}. FT REGION 153 156 G4. {ECO:0000250}. FT REGION 194 196 G5. {ECO:0000250}. FT MOD_RES 36 36 N6,N6,N6-trimethyllysine. FT {ECO:0000250|UniProtKB:P68105}. FT MOD_RES 55 55 N6,N6-dimethyllysine. FT {ECO:0000269|Ref.7}. FT MOD_RES 79 79 N6,N6,N6-trimethyllysine. FT {ECO:0000250|UniProtKB:P68105}. FT MOD_RES 165 165 N6,N6-dimethyllysine; alternate. FT {ECO:0000269|Ref.7}. FT MOD_RES 165 165 N6-acetyllysine; alternate. FT {ECO:0000250|UniProtKB:P10126}. FT MOD_RES 172 172 N6-acetyllysine. FT {ECO:0000250|UniProtKB:P10126}. FT MOD_RES 273 273 N6-acetyllysine. FT {ECO:0000250|UniProtKB:P10126}. FT MOD_RES 300 300 Phosphoserine; by TGFBR1. FT {ECO:0000269|PubMed:20832312}. FT MOD_RES 301 301 5-glutamyl FT glycerylphosphorylethanolamine. FT {ECO:0000269|PubMed:2569467}. FT MOD_RES 318 318 N6,N6,N6-trimethyllysine. FT {ECO:0000250|UniProtKB:P68105}. FT MOD_RES 374 374 5-glutamyl FT glycerylphosphorylethanolamine. FT {ECO:0000269|PubMed:2569467}. FT MOD_RES 392 392 N6-acetyllysine; alternate. FT {ECO:0000250|UniProtKB:P10126}. FT MOD_RES 392 392 N6-succinyllysine; alternate. FT {ECO:0000250|UniProtKB:P10126}. FT MOD_RES 432 432 Phosphothreonine; by PASK. FT {ECO:0000269|PubMed:17595531}. FT MOD_RES 439 439 N6-acetyllysine. FT {ECO:0000250|UniProtKB:P10126}. FT VAR_SEQ 141 161 Missing (in isoform 2). FT {ECO:0000303|PubMed:15489334}. FT /FTId=VSP_057184. FT MUTAGEN 432 432 T->A: Abolishes phosphorylation by PASK. FT {ECO:0000269|PubMed:17595531}. FT CONFLICT 83 83 S -> A (in Ref. 6; CAA27325). FT {ECO:0000305}. FT CONFLICT 232 232 L -> V (in Ref. 3; CAA34756). FT {ECO:0000305}. 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 //