##gff-version 3 P46462 UniProtKB Initiator methionine 1 1 . . . Note=Removed;Ontology_term=ECO:0000250;evidence=ECO:0000250|UniProtKB:P55072 P46462 UniProtKB Chain 2 806 . . . ID=PRO_0000084575;Note=Transitional endoplasmic reticulum ATPase P46462 UniProtKB Region 708 727 . . . Note=Disordered;Ontology_term=ECO:0000256;evidence=ECO:0000256|SAM:MobiDB-lite P46462 UniProtKB Region 768 806 . . . Note=Disordered;Ontology_term=ECO:0000256;evidence=ECO:0000256|SAM:MobiDB-lite P46462 UniProtKB Region 797 806 . . . Note=Interaction with UBXN6;Ontology_term=ECO:0000250;evidence=ECO:0000250 P46462 UniProtKB Motif 802 806 . . . Note=PIM motif;Ontology_term=ECO:0000250;evidence=ECO:0000250|UniProtKB:P55072 P46462 UniProtKB Compositional bias 768 794 . . . Note=Polar residues;Ontology_term=ECO:0000256;evidence=ECO:0000256|SAM:MobiDB-lite P46462 UniProtKB Binding site 247 253 . . . Ontology_term=ECO:0000250;evidence=ECO:0000250|UniProtKB:P55072 P46462 UniProtKB Binding site 348 348 . . . Ontology_term=ECO:0000250;evidence=ECO:0000250|UniProtKB:P55072 P46462 UniProtKB Binding site 384 384 . . . Ontology_term=ECO:0000250;evidence=ECO:0000250|UniProtKB:P55072 P46462 UniProtKB Binding site 521 526 . . . Ontology_term=ECO:0000250;evidence=ECO:0000250|UniProtKB:Q01853 P46462 UniProtKB Modified residue 2 2 . . . Note=N-acetylalanine;Ontology_term=ECO:0000250;evidence=ECO:0000250|UniProtKB:P55072 P46462 UniProtKB Modified residue 3 3 . . . Note=Phosphoserine;Ontology_term=ECO:0007744;evidence=ECO:0007744|PubMed:22673903;Dbxref=PMID:22673903 P46462 UniProtKB Modified residue 7 7 . . . Note=Phosphoserine;Ontology_term=ECO:0007744;evidence=ECO:0007744|PubMed:22673903;Dbxref=PMID:22673903 P46462 UniProtKB Modified residue 13 13 . . . Note=Phosphoserine;Ontology_term=ECO:0000250;evidence=ECO:0000250|UniProtKB:P55072 P46462 UniProtKB Modified residue 37 37 . . . Note=Phosphoserine;Ontology_term=ECO:0000250;evidence=ECO:0000250|UniProtKB:P55072 P46462 UniProtKB Modified residue 315 315 . . . Note=N6%2CN6%2CN6-trimethyllysine%3B by VCPKMT;Ontology_term=ECO:0000250;evidence=ECO:0000250|UniProtKB:P55072 P46462 UniProtKB Modified residue 436 436 . . . Note=Phosphothreonine;Ontology_term=ECO:0000250;evidence=ECO:0000250|UniProtKB:P55072 P46462 UniProtKB Modified residue 462 462 . . . Note=Phosphoserine;Ontology_term=ECO:0000250;evidence=ECO:0000250|UniProtKB:P55072 P46462 UniProtKB Modified residue 502 502 . . . Note=N6-acetyllysine;Ontology_term=ECO:0000250;evidence=ECO:0000250|UniProtKB:Q01853 P46462 UniProtKB Modified residue 505 505 . . . Note=N6-acetyllysine;Ontology_term=ECO:0000250;evidence=ECO:0000250|UniProtKB:Q01853 P46462 UniProtKB Modified residue 668 668 . . . Note=N6-acetyllysine%3B alternate;Ontology_term=ECO:0000250;evidence=ECO:0000250|UniProtKB:Q01853 P46462 UniProtKB Modified residue 668 668 . . . Note=N6-succinyllysine%3B alternate;Ontology_term=ECO:0000250;evidence=ECO:0000250|UniProtKB:Q01853 P46462 UniProtKB Modified residue 702 702 . . . Note=Phosphoserine;Ontology_term=ECO:0000250;evidence=ECO:0000250|UniProtKB:P55072 P46462 UniProtKB Modified residue 754 754 . . . Note=N6-acetyllysine;Ontology_term=ECO:0000250;evidence=ECO:0000250|UniProtKB:Q01853 P46462 UniProtKB Modified residue 770 770 . . . Note=Phosphoserine;Ontology_term=ECO:0000250;evidence=ECO:0000250|UniProtKB:P55072 P46462 UniProtKB Modified residue 775 775 . . . Note=Phosphoserine;Ontology_term=ECO:0000250;evidence=ECO:0000250|UniProtKB:P55072 P46462 UniProtKB Modified residue 787 787 . . . Note=Phosphoserine;Ontology_term=ECO:0000250;evidence=ECO:0000250|UniProtKB:P55072 P46462 UniProtKB Modified residue 805 805 . . . Note=Phosphotyrosine;Ontology_term=ECO:0000250;evidence=ECO:0000250|UniProtKB:Q01853 P46462 UniProtKB Cross-link 8 8 . . . Note=Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO2);Ontology_term=ECO:0000250;evidence=ECO:0000250|UniProtKB:P55072 P46462 UniProtKB Cross-link 18 18 . . . Note=Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO2);Ontology_term=ECO:0000250;evidence=ECO:0000250|UniProtKB:P55072