##gff-version 3 P20029 UniProtKB Signal peptide 1 19 . . . Ontology_term=ECO:0000269,ECO:0000269;evidence=ECO:0000269|PubMed:2559088,ECO:0000269|PubMed:7523108;Dbxref=PMID:2559088,PMID:7523108 P20029 UniProtKB Chain 20 655 . . . ID=PRO_0000013568;Note=Endoplasmic reticulum chaperone BiP P20029 UniProtKB Region 1 81 . . . Note=Required for interaction with KIAA1324;Ontology_term=ECO:0000250;evidence=ECO:0000250|UniProtKB:P11021 P20029 UniProtKB Region 126 281 . . . Note=Nucleotide-binding (NBD);Ontology_term=ECO:0000250;evidence=ECO:0000250|UniProtKB:P11021 P20029 UniProtKB Region 410 420 . . . Note=Interdomain linker;Ontology_term=ECO:0000250;evidence=ECO:0000250|UniProtKB:G3I8R9 P20029 UniProtKB Region 421 501 . . . Note=Substrate-binding (SBD);Ontology_term=ECO:0000250;evidence=ECO:0000250|UniProtKB:P11021 P20029 UniProtKB Region 632 655 . . . Note=Disordered;Ontology_term=ECO:0000256;evidence=ECO:0000256|SAM:MobiDB-lite P20029 UniProtKB Motif 652 655 . . . Note=Prevents secretion from ER P20029 UniProtKB Binding site 37 40 . . . Ontology_term=ECO:0000250;evidence=ECO:0000250|UniProtKB:P11021 P20029 UniProtKB Binding site 97 97 . . . Ontology_term=ECO:0000250;evidence=ECO:0000250|UniProtKB:P11021 P20029 UniProtKB Binding site 228 230 . . . Ontology_term=ECO:0000250;evidence=ECO:0000250|UniProtKB:P11021 P20029 UniProtKB Binding site 294 301 . . . Ontology_term=ECO:0000250;evidence=ECO:0000250|UniProtKB:P11021 P20029 UniProtKB Binding site 365 368 . . . Ontology_term=ECO:0000250;evidence=ECO:0000250|UniProtKB:P11021 P20029 UniProtKB Modified residue 87 87 . . . Note=Phosphoserine;Ontology_term=ECO:0000250;evidence=ECO:0000250|UniProtKB:P06761 P20029 UniProtKB Modified residue 126 126 . . . Note=N6-acetyllysine;Ontology_term=ECO:0007744;evidence=ECO:0007744|PubMed:23806337;Dbxref=PMID:23806337 P20029 UniProtKB Modified residue 161 161 . . . Note=3'-nitrotyrosine;Ontology_term=ECO:0007744;evidence=ECO:0007744|PubMed:16800626;Dbxref=PMID:16800626 P20029 UniProtKB Modified residue 214 214 . . . Note=N6-acetyllysine;Ontology_term=ECO:0007744;evidence=ECO:0007744|PubMed:23806337;Dbxref=PMID:23806337 P20029 UniProtKB Modified residue 272 272 . . . Note=N6-acetyllysine;Ontology_term=ECO:0000250;evidence=ECO:0000250|UniProtKB:P0DMV8 P20029 UniProtKB Modified residue 327 327 . . . Note=N6-acetyllysine;Ontology_term=ECO:0007744;evidence=ECO:0007744|PubMed:23806337;Dbxref=PMID:23806337 P20029 UniProtKB Modified residue 354 354 . . . Note=N6-acetyllysine%3B alternate;Ontology_term=ECO:0007744;evidence=ECO:0007744|PubMed:23806337;Dbxref=PMID:23806337 P20029 UniProtKB Modified residue 448 448 . . . Note=N6-succinyllysine;Ontology_term=ECO:0007744;evidence=ECO:0007744|PubMed:23806337;Dbxref=PMID:23806337 P20029 UniProtKB Modified residue 493 493 . . . Note=Omega-N-methylarginine;Ontology_term=ECO:0000250;evidence=ECO:0000250|UniProtKB:P0DMV8 P20029 UniProtKB Modified residue 519 519 . . . Note=O-AMP-threonine%3B alternate;Ontology_term=ECO:0000250;evidence=ECO:0000250|UniProtKB:G3I8R9 P20029 UniProtKB Modified residue 519 519 . . . Note=Phosphothreonine%3B alternate;Ontology_term=ECO:0000250;evidence=ECO:0000250|UniProtKB:P11021 P20029 UniProtKB Modified residue 586 586 . . . Note=N6%2CN6%2CN6-trimethyllysine%3B by METTL21A%3B in vitro;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:23921388;Dbxref=PMID:23921388 P20029 UniProtKB Modified residue 586 586 . . . Note=N6%2CN6-dimethyllysine%3B alternate;Ontology_term=ECO:0000250;evidence=ECO:0000250|UniProtKB:P11021 P20029 UniProtKB Modified residue 586 586 . . . Note=N6-methyllysine%3B alternate;Ontology_term=ECO:0000250;evidence=ECO:0000250|UniProtKB:P11021 P20029 UniProtKB Modified residue 592 592 . . . Note=N6-methyllysine;Ontology_term=ECO:0000250;evidence=ECO:0000250|UniProtKB:P11021 P20029 UniProtKB Modified residue 644 644 . . . Note=Phosphothreonine;Ontology_term=ECO:0007744;evidence=ECO:0007744|PubMed:21183079;Dbxref=PMID:21183079 P20029 UniProtKB Modified residue 649 649 . . . Note=Phosphothreonine;Ontology_term=ECO:0007744;evidence=ECO:0007744|PubMed:21183079;Dbxref=PMID:21183079 P20029 UniProtKB Modified residue 650 650 . . . Note=Phosphoserine;Ontology_term=ECO:0007744,ECO:0007744;evidence=ECO:0007744|PubMed:17242355,ECO:0007744|PubMed:21183079;Dbxref=PMID:17242355,PMID:21183079 P20029 UniProtKB Cross-link 353 353 . . . Note=Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO2);Ontology_term=ECO:0000250;evidence=ECO:0000250|UniProtKB:P11021 P20029 UniProtKB Cross-link 354 354 . . . Note=Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO1)%3B alternate;Ontology_term=ECO:0000250;evidence=ECO:0000250|UniProtKB:P11021 P20029 UniProtKB Sequence conflict 43 43 . . . Note=V->F;Ontology_term=ECO:0000305;evidence=ECO:0000305 P20029 UniProtKB Sequence conflict 245 245 . . . Note=V->W;Ontology_term=ECO:0000305;evidence=ECO:0000305 P20029 UniProtKB Sequence conflict 329 329 . . . Note=E->G;Ontology_term=ECO:0000305;evidence=ECO:0000305 P20029 UniProtKB Sequence conflict 361 361 . . . Note=V->A;Ontology_term=ECO:0000305;evidence=ECO:0000305 P20029 UniProtKB Sequence conflict 474 474 . . . Note=T->R;Ontology_term=ECO:0000305;evidence=ECO:0000305 P20029 UniProtKB Sequence conflict 591 591 . . . Note=D->G;Ontology_term=ECO:0000305;evidence=ECO:0000305 P20029 UniProtKB Sequence conflict 596 596 . . . Note=E->K;Ontology_term=ECO:0000305;evidence=ECO:0000305