##gff-version 3 Q8NE71 UniProtKB Chain 1 845 . . . ID=PRO_0000093318;Note=ATP-binding cassette sub-family F member 1 Q8NE71 UniProtKB Domain 304 548 . . . Note=ABC transporter 1;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00434 Q8NE71 UniProtKB Domain 625 840 . . . Note=ABC transporter 2;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00434 Q8NE71 UniProtKB Region 1 261 . . . Note=Disordered;Ontology_term=ECO:0000256;evidence=ECO:0000256|SAM:MobiDB-lite Q8NE71 UniProtKB Region 559 602 . . . Note=Disordered;Ontology_term=ECO:0000256;evidence=ECO:0000256|SAM:MobiDB-lite Q8NE71 UniProtKB Compositional bias 37 63 . . . Note=Basic and acidic residues;Ontology_term=ECO:0000256;evidence=ECO:0000256|SAM:MobiDB-lite Q8NE71 UniProtKB Compositional bias 83 121 . . . Note=Basic and acidic residues;Ontology_term=ECO:0000256;evidence=ECO:0000256|SAM:MobiDB-lite Q8NE71 UniProtKB Compositional bias 145 198 . . . Note=Basic and acidic residues;Ontology_term=ECO:0000256;evidence=ECO:0000256|SAM:MobiDB-lite Q8NE71 UniProtKB Compositional bias 207 229 . . . Note=Basic and acidic residues;Ontology_term=ECO:0000256;evidence=ECO:0000256|SAM:MobiDB-lite Q8NE71 UniProtKB Compositional bias 230 244 . . . Note=Acidic residues;Ontology_term=ECO:0000256;evidence=ECO:0000256|SAM:MobiDB-lite Q8NE71 UniProtKB Compositional bias 245 261 . . . Note=Basic and acidic residues;Ontology_term=ECO:0000256;evidence=ECO:0000256|SAM:MobiDB-lite Q8NE71 UniProtKB Binding site 336 343 . . . Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00434 Q8NE71 UniProtKB Binding site 658 665 . . . Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00434 Q8NE71 UniProtKB Modified residue 22 22 . . . Note=Phosphoserine;Ontology_term=ECO:0007744,ECO:0007744;evidence=ECO:0007744|PubMed:20068231,ECO:0007744|PubMed:23186163;Dbxref=PMID:20068231,PMID:23186163 Q8NE71 UniProtKB Modified residue 24 24 . . . Note=Phosphoserine;Ontology_term=ECO:0007744;evidence=ECO:0007744|PubMed:18669648;Dbxref=PMID:18669648 Q8NE71 UniProtKB Modified residue 105 105 . . . Note=Phosphoserine;Ontology_term=ECO:0007744,ECO:0007744,ECO:0007744,ECO:0007744;evidence=ECO:0007744|PubMed:17081983,ECO:0007744|PubMed:20068231,ECO:0007744|PubMed:23186163,ECO:0007744|PubMed:24275569;Dbxref=PMID:17081983,PMID:20068231,PMID:23186163,PMID:24275569 Q8NE71 UniProtKB Modified residue 108 108 . . . Note=Phosphothreonine;Ontology_term=ECO:0007744,ECO:0007744,ECO:0007744,ECO:0007744,ECO:0007744,ECO:0007744;evidence=ECO:0007744|PubMed:17081983,ECO:0007744|PubMed:19690332,ECO:0007744|PubMed:20068231,ECO:0007744|PubMed:21406692,ECO:0007744|PubMed:23186163,ECO:0007744|PubMed:24275569;Dbxref=PMID:17081983,PMID:19690332,PMID:20068231,PMID:21406692,PMID:23186163,PMID:24275569 Q8NE71 UniProtKB Modified residue 109 109 . . . Note=Phosphoserine%3B by CK2;Ontology_term=ECO:0000269,ECO:0007744,ECO:0007744,ECO:0007744,ECO:0007744,ECO:0007744;evidence=ECO:0000269|PubMed:17894550,ECO:0007744|PubMed:17081983,ECO:0007744|PubMed:19690332,ECO:0007744|PubMed:20068231,ECO:0007744|PubMed:21406692,ECO:0007744|PubMed:23186163;Dbxref=PMID:17081983,PMID:17894550,PMID:19690332,PMID:20068231,PMID:21406692,PMID:23186163 Q8NE71 UniProtKB Modified residue 140 140 . . . Note=Phosphoserine%3B by CK2;Ontology_term=ECO:0000269,ECO:0007744,ECO:0007744,ECO:0007744,ECO:0007744,ECO:0007744;evidence=ECO:0000269|PubMed:17894550,ECO:0007744|PubMed:17081983,ECO:0007744|PubMed:19690332,ECO:0007744|PubMed:20068231,ECO:0007744|PubMed:21406692,ECO:0007744|PubMed:23186163;Dbxref=PMID:17081983,PMID:17894550,PMID:19690332,PMID:20068231,PMID:21406692,PMID:23186163 Q8NE71 UniProtKB Modified residue 166 166 . . . Note=Phosphoserine;Ontology_term=ECO:0007744,ECO:0007744;evidence=ECO:0007744|PubMed:21406692,ECO:0007744|PubMed:23186163;Dbxref=PMID:21406692,PMID:23186163 Q8NE71 UniProtKB Modified residue 228 228 . . . Note=Phosphoserine;Ontology_term=ECO:0007744,ECO:0007744,ECO:0007744,ECO:0007744,ECO:0007744,ECO:0007744,ECO:0007744,ECO:0007744;evidence=ECO:0007744|PubMed:16964243,ECO:0007744|PubMed:17081983,ECO:0007744|PubMed:18318008,ECO:0007744|PubMed:18669648,ECO:0007744|PubMed:19690332,ECO:0007744|PubMed:20068231,ECO:0007744|PubMed:21406692,ECO:0007744|PubMed:23186163;Dbxref=PMID:16964243,PMID:17081983,PMID:18318008,PMID:18669648,PMID:19690332,PMID:20068231,PMID:21406692,PMID:23186163 Q8NE71 UniProtKB Modified residue 595 595 . . . Note=Phosphoserine;Ontology_term=ECO:0007744,ECO:0007744;evidence=ECO:0007744|PubMed:17525332,ECO:0007744|PubMed:23186163;Dbxref=PMID:17525332,PMID:23186163 Q8NE71 UniProtKB Alternative sequence 226 263 . . . ID=VSP_012078;Note=In isoform 2. Missing;Ontology_term=ECO:0000303;evidence=ECO:0000303|PubMed:9790762;Dbxref=PMID:9790762 Q8NE71 UniProtKB Natural variant 198 198 . . . ID=VAR_048136;Note=N->D;Dbxref=dbSNP:rs6902544 Q8NE71 UniProtKB Mutagenesis 109 109 . . . Note=Reduces phosphorylation. Inhibits strongly phosphorylation by CK2%3B when associated with S-140. Does not inhibit interaction with EIF2%3B when associated with S-140. Does not inhibit association with ribosomes%3B when associated with S-140. Reduces EIF2 interaction with ribosomes%3B when associated with S-140. Does not inhibit protein synthesis%3B when associated with A-140. S->A;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:17894550;Dbxref=PMID:17894550 Q8NE71 UniProtKB Mutagenesis 140 140 . . . Note=Reduces phosphorylation. Inhibits strongly phosphorylation by CK2%3B when associated with S-109. Does not inhibits interaction with EIF2%3B when associated with S-109. Does not inhibit association with ribosomes%3B when associated with S-109. Reduces EIF2 interaction with ribosomes%3B when associated with S-109. Does not inhibit protein synthesis%3B when associated with A-109. S->A;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:17894550;Dbxref=PMID:17894550 Q8NE71 UniProtKB Mutagenesis 342 342 . . . Note=Does not inhibit ribosome binding. Reduces ATP-binding. Inhibits ATP-binding and reduces protein synthesis%3B when associated with M-664. Shows an enhanced association with polyribosomes%3B when associated with M-664. Does not inhibit IRES-mediated protein synthesis%3B when associated with M-664. K->M;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:19570978;Dbxref=PMID:19570978 Q8NE71 UniProtKB Mutagenesis 367 367 . . . Note=Does not inhibit ribosome binding. Q->E;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:19570978;Dbxref=PMID:19570978 Q8NE71 UniProtKB Mutagenesis 454 454 . . . Note=Does not inhibit ribosome binding. G->D;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:19570978;Dbxref=PMID:19570978 Q8NE71 UniProtKB Mutagenesis 477 477 . . . Note=Does not inhibit ribosome binding. Reduces protein synthesis%3B when associated with Q-768. E->Q;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:19570978;Dbxref=PMID:19570978 Q8NE71 UniProtKB Mutagenesis 506 506 . . . Note=Does not inhibit ribosome binding. H->L;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:19570978;Dbxref=PMID:19570978 Q8NE71 UniProtKB Mutagenesis 664 664 . . . Note=Does not inhibit ribosome binding. Reduces ATP-binding. Inhibits ATP-binding and reduces protein synthesis%3B when associated with M-342. Shows a reduced association with polyribosomes%3B when associated with M-664. Does not inhibit IRES-mediated protein synthesis%3B when associated with M-664. K->M;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:19570978;Dbxref=PMID:19570978 Q8NE71 UniProtKB Mutagenesis 695 695 . . . Note=Does not inhibit ribosome binding. Q->E;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:19570978;Dbxref=PMID:19570978 Q8NE71 UniProtKB Mutagenesis 745 745 . . . Note=Does not inhibit ribosome binding. G->D;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:19570978;Dbxref=PMID:19570978 Q8NE71 UniProtKB Mutagenesis 768 768 . . . Note=Does not inhibit ribosome binding. Reduces protein synthesis%3B when associated with Q-477. E->Q;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:19570978;Dbxref=PMID:19570978 Q8NE71 UniProtKB Mutagenesis 797 797 . . . Note=Does not inhibit ribosome binding. H->L;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:19570978;Dbxref=PMID:19570978 Q8NE71 UniProtKB Sequence conflict 166 166 . . . Note=S->P;Ontology_term=ECO:0000305;evidence=ECO:0000305 Q8NE71 UniProtKB Beta strand 304 313 . . . Ontology_term=ECO:0007829;evidence=ECO:0007829|PDB:5ZXD Q8NE71 UniProtKB Beta strand 316 326 . . . Ontology_term=ECO:0007829;evidence=ECO:0007829|PDB:5ZXD Q8NE71 UniProtKB Beta strand 331 335 . . . Ontology_term=ECO:0007829;evidence=ECO:0007829|PDB:5ZXD Q8NE71 UniProtKB Helix 342 350 . . . Ontology_term=ECO:0007829;evidence=ECO:0007829|PDB:5ZXD Q8NE71 UniProtKB Beta strand 361 363 . . . Ontology_term=ECO:0007829;evidence=ECO:0007829|PDB:5ZXD Q8NE71 UniProtKB Helix 374 379 . . . Ontology_term=ECO:0007829;evidence=ECO:0007829|PDB:5ZXD Q8NE71 UniProtKB Helix 383 403 . . . Ontology_term=ECO:0007829;evidence=ECO:0007829|PDB:5ZXD Q8NE71 UniProtKB Helix 408 419 . . . Ontology_term=ECO:0007829;evidence=ECO:0007829|PDB:5ZXD Q8NE71 UniProtKB Helix 424 437 . . . Ontology_term=ECO:0007829;evidence=ECO:0007829|PDB:5ZXD Q8NE71 UniProtKB Helix 442 445 . . . Ontology_term=ECO:0007829;evidence=ECO:0007829|PDB:5ZXD Q8NE71 UniProtKB Helix 449 451 . . . Ontology_term=ECO:0007829;evidence=ECO:0007829|PDB:5ZXD Q8NE71 UniProtKB Helix 454 468 . . . Ontology_term=ECO:0007829;evidence=ECO:0007829|PDB:5ZXD Q8NE71 UniProtKB Beta strand 471 477 . . . Ontology_term=ECO:0007829;evidence=ECO:0007829|PDB:5ZXD Q8NE71 UniProtKB Turn 478 481 . . . Ontology_term=ECO:0007829;evidence=ECO:0007829|PDB:5ZXD Q8NE71 UniProtKB Helix 484 495 . . . Ontology_term=ECO:0007829;evidence=ECO:0007829|PDB:5ZXD Q8NE71 UniProtKB Beta strand 499 504 . . . Ontology_term=ECO:0007829;evidence=ECO:0007829|PDB:5ZXD Q8NE71 UniProtKB Helix 508 514 . . . Ontology_term=ECO:0007829;evidence=ECO:0007829|PDB:5ZXD Q8NE71 UniProtKB Beta strand 516 522 . . . Ontology_term=ECO:0007829;evidence=ECO:0007829|PDB:5ZXD Q8NE71 UniProtKB Beta strand 525 531 . . . Ontology_term=ECO:0007829;evidence=ECO:0007829|PDB:5ZXD Q8NE71 UniProtKB Helix 533 563 . . . Ontology_term=ECO:0007829;evidence=ECO:0007829|PDB:5ZXD Q8NE71 UniProtKB Beta strand 625 632 . . . Ontology_term=ECO:0007829;evidence=ECO:0007829|PDB:5ZXD Q8NE71 UniProtKB Beta strand 640 648 . . . Ontology_term=ECO:0007829;evidence=ECO:0007829|PDB:5ZXD Q8NE71 UniProtKB Beta strand 653 657 . . . Ontology_term=ECO:0007829;evidence=ECO:0007829|PDB:5ZXD Q8NE71 UniProtKB Helix 664 672 . . . Ontology_term=ECO:0007829;evidence=ECO:0007829|PDB:5ZXD Q8NE71 UniProtKB Beta strand 673 675 . . . Ontology_term=ECO:0007829;evidence=ECO:0007829|PDB:5ZXD Q8NE71 UniProtKB Beta strand 678 684 . . . Ontology_term=ECO:0007829;evidence=ECO:0007829|PDB:5ZXD Q8NE71 UniProtKB Beta strand 690 693 . . . Ontology_term=ECO:0007829;evidence=ECO:0007829|PDB:5ZXD Q8NE71 UniProtKB Helix 695 698 . . . Ontology_term=ECO:0007829;evidence=ECO:0007829|PDB:5ZXD Q8NE71 UniProtKB Helix 707 715 . . . Ontology_term=ECO:0007829;evidence=ECO:0007829|PDB:5ZXD Q8NE71 UniProtKB Helix 719 728 . . . Ontology_term=ECO:0007829;evidence=ECO:0007829|PDB:5ZXD Q8NE71 UniProtKB Helix 733 737 . . . Ontology_term=ECO:0007829;evidence=ECO:0007829|PDB:5ZXD Q8NE71 UniProtKB Helix 740 742 . . . Ontology_term=ECO:0007829;evidence=ECO:0007829|PDB:5ZXD Q8NE71 UniProtKB Helix 745 758 . . . Ontology_term=ECO:0007829;evidence=ECO:0007829|PDB:5ZXD Q8NE71 UniProtKB Beta strand 762 768 . . . Ontology_term=ECO:0007829;evidence=ECO:0007829|PDB:5ZXD Q8NE71 UniProtKB Turn 769 772 . . . Ontology_term=ECO:0007829;evidence=ECO:0007829|PDB:5ZXD Q8NE71 UniProtKB Helix 775 787 . . . Ontology_term=ECO:0007829;evidence=ECO:0007829|PDB:5ZXD Q8NE71 UniProtKB Beta strand 790 795 . . . Ontology_term=ECO:0007829;evidence=ECO:0007829|PDB:5ZXD Q8NE71 UniProtKB Helix 799 804 . . . Ontology_term=ECO:0007829;evidence=ECO:0007829|PDB:5ZXD Q8NE71 UniProtKB Beta strand 808 813 . . . Ontology_term=ECO:0007829;evidence=ECO:0007829|PDB:5ZXD Q8NE71 UniProtKB Beta strand 816 820 . . . Ontology_term=ECO:0007829;evidence=ECO:0007829|PDB:5ZXD Q8NE71 UniProtKB Helix 824 834 . . . Ontology_term=ECO:0007829;evidence=ECO:0007829|PDB:5ZXD