##gff-version 3 P68104 UniProtKB Initiator methionine 1 1 . . . Note=Removed;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:26545399;Dbxref=PMID:26545399 P68104 UniProtKB Chain 2 462 . . . ID=PRO_0000090885;Note=Elongation factor 1-alpha 1 P68104 UniProtKB Domain 5 242 . . . Note=Tr-type G P68104 UniProtKB Region 14 21 . . . Note=G1;Ontology_term=ECO:0000255;evidence=ECO:0000255 P68104 UniProtKB Region 70 74 . . . Note=G2;Ontology_term=ECO:0000255;evidence=ECO:0000255 P68104 UniProtKB Region 91 94 . . . Note=G3;Ontology_term=ECO:0000255;evidence=ECO:0000255 P68104 UniProtKB Region 153 156 . . . Note=G4;Ontology_term=ECO:0000255;evidence=ECO:0000255 P68104 UniProtKB Region 194 196 . . . Note=G5;Ontology_term=ECO:0000255;evidence=ECO:0000255 P68104 UniProtKB Binding site 14 21 . . . Ontology_term=ECO:0000250;evidence=ECO:0000250|UniProtKB:P68105 P68104 UniProtKB Binding site 153 156 . . . Ontology_term=ECO:0000250;evidence=ECO:0000250|UniProtKB:P68105 P68104 UniProtKB Binding site 194 196 . . . Ontology_term=ECO:0000250;evidence=ECO:0000250|UniProtKB:P68105 P68104 UniProtKB Modified residue 2 2 . . . Note=N%2CN%2CN-trimethylglycine;Ontology_term=ECO:0000269,ECO:0000269;evidence=ECO:0000269|PubMed:26545399,ECO:0000269|PubMed:30143613;Dbxref=PMID:26545399,PMID:30143613 P68104 UniProtKB Modified residue 36 36 . . . Note=N6%2CN6%2CN6-trimethyllysine%3B alternate%3B by EEF1AKMT4;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:28520920;Dbxref=PMID:28520920 P68104 UniProtKB Modified residue 36 36 . . . Note=N6%2CN6-dimethyllysine%3B alternate%3B by EEF1AKMT4;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:28520920;Dbxref=PMID:28520920 P68104 UniProtKB Modified residue 36 36 . . . Note=N6-methyllysine%3B alternate%3B by EEF1AKMT4;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:28520920;Dbxref=PMID:28520920 P68104 UniProtKB Modified residue 55 55 . . . Note=N6%2CN6-dimethyllysine;Ontology_term=ECO:0000269,ECO:0000269,ECO:0000269;evidence=ECO:0000269|PubMed:30143613,ECO:0000269|PubMed:30612740,ECO:0000269|Ref.7;Dbxref=PMID:30143613,PMID:30612740 P68104 UniProtKB Modified residue 79 79 . . . Note=N6%2CN6%2CN6-trimethyllysine%3B by EEF1AKMT1;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:26545399;Dbxref=PMID:26545399 P68104 UniProtKB Modified residue 165 165 . . . Note=N6%2CN6%2CN6-trimethyllysine%3B alternate%3B by EEF1AKMT3;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:28108655;Dbxref=PMID:28108655 P68104 UniProtKB Modified residue 165 165 . . . Note=N6%2CN6-dimethyllysine%3B alternate%3B by EEF1AKMT3;Ontology_term=ECO:0000269,ECO:0000269;evidence=ECO:0000269|PubMed:28108655,ECO:0000269|Ref.7;Dbxref=PMID:28108655 P68104 UniProtKB Modified residue 165 165 . . . Note=N6-acetyllysine%3B alternate;Ontology_term=ECO:0000250;evidence=ECO:0000250|UniProtKB:P10126 P68104 UniProtKB Modified residue 165 165 . . . Note=N6-methyllysine%3B alternate%3B by EEF1AKMT3;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:28108655;Dbxref=PMID:28108655 P68104 UniProtKB Modified residue 172 172 . . . Note=N6-acetyllysine;Ontology_term=ECO:0000250;evidence=ECO:0000250|UniProtKB:P10126 P68104 UniProtKB Modified residue 273 273 . . . Note=N6-acetyllysine;Ontology_term=ECO:0000250;evidence=ECO:0000250|UniProtKB:P10126 P68104 UniProtKB Modified residue 300 300 . . . Note=Phosphoserine%3B by TGFBR1;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:20832312;Dbxref=PMID:20832312 P68104 UniProtKB Modified residue 301 301 . . . Note=5-glutamyl glycerylphosphorylethanolamine;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:2569467;Dbxref=PMID:2569467 P68104 UniProtKB Modified residue 318 318 . . . Note=N6%2CN6%2CN6-trimethyllysine%3B by EEF1AKMT2;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:25144183;Dbxref=PMID:25144183 P68104 UniProtKB Modified residue 374 374 . . . Note=5-glutamyl glycerylphosphorylethanolamine;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:2569467;Dbxref=PMID:2569467 P68104 UniProtKB Modified residue 392 392 . . . Note=N6-acetyllysine%3B alternate;Ontology_term=ECO:0000250;evidence=ECO:0000250|UniProtKB:P10126 P68104 UniProtKB Modified residue 392 392 . . . Note=N6-succinyllysine%3B alternate;Ontology_term=ECO:0000250;evidence=ECO:0000250|UniProtKB:P10126 P68104 UniProtKB Modified residue 432 432 . . . Note=Phosphothreonine%3B by PASK;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:17595531;Dbxref=PMID:17595531 P68104 UniProtKB Modified residue 439 439 . . . Note=N6-acetyllysine;Ontology_term=ECO:0000250;evidence=ECO:0000250|UniProtKB:P10126 P68104 UniProtKB Cross-link 385 385 . . . Note=Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin);Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:36638793;Dbxref=PMID:36638793 P68104 UniProtKB Mutagenesis 36 36 . . . Note=No effect on methylation by EEF1AKMT2. Abolishes EEF1AKMT4-mediated methylation. K->R;Ontology_term=ECO:0000269,ECO:0000269;evidence=ECO:0000269|PubMed:25144183,ECO:0000269|PubMed:28520920;Dbxref=PMID:25144183,PMID:28520920 P68104 UniProtKB Mutagenesis 55 55 . . . Note=No effect on methylation by EEF1AKMT2. Abolishes methylation by METTL13. K->R;Ontology_term=ECO:0000269,ECO:0000269,ECO:0000269;evidence=ECO:0000269|PubMed:25144183,ECO:0000269|PubMed:30143613,ECO:0000269|PubMed:30612740;Dbxref=PMID:25144183,PMID:30143613,PMID:30612740 P68104 UniProtKB Mutagenesis 79 79 . . . Note=No effect on methylation by EEF1AKMT2. K->R;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:25144183;Dbxref=PMID:25144183 P68104 UniProtKB Mutagenesis 165 165 . . . Note=Abolishes methylation by EEF1AKMT3. K->A;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:28108655;Dbxref=PMID:28108655 P68104 UniProtKB Mutagenesis 165 165 . . . Note=No effect on methylation by EEF1AKMT2. K->R;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:25144183;Dbxref=PMID:25144183 P68104 UniProtKB Mutagenesis 318 318 . . . Note=Abolishes methylation by EEF1AKMT2. K->R;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:25144183;Dbxref=PMID:25144183 P68104 UniProtKB Mutagenesis 385 385 . . . Note=Impaired ubiquitination in response to ribosome stalling caused by ternatin-4. K->R;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:36638793;Dbxref=PMID:36638793 P68104 UniProtKB Mutagenesis 399 399 . . . Note=Resistant to inhibition by plitidepsin and ternatin-4. No effect on SARS-CoV-2 proteins translation. A->V;Ontology_term=ECO:0000269,ECO:0000269,ECO:0000269;evidence=ECO:0000269|PubMed:26651998,ECO:0000269|PubMed:33495306,ECO:0000269|PubMed:36264623;Dbxref=PMID:26651998,PMID:33495306,PMID:36264623 P68104 UniProtKB Mutagenesis 432 432 . . . Note=Abolishes phosphorylation by PASK. T->A;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:17595531;Dbxref=PMID:17595531 P68104 UniProtKB Sequence conflict 83 83 . . . Note=S->A;Ontology_term=ECO:0000305;evidence=ECO:0000305 P68104 UniProtKB Sequence conflict 232 232 . . . Note=L->V;Ontology_term=ECO:0000305;evidence=ECO:0000305