##gff-version 3 O88339 UniProtKB Chain 1 575 . . . ID=PRO_0000074515;Note=Epsin-1 O88339 UniProtKB Domain 12 144 . . . Note=ENTH;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00243 O88339 UniProtKB Domain 183 202 . . . Note=UIM 1;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00213 O88339 UniProtKB Domain 208 227 . . . Note=UIM 2;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00213 O88339 UniProtKB Domain 233 252 . . . Note=UIM 3;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00213 O88339 UniProtKB Repeat 274 276 . . . Note=1 O88339 UniProtKB Repeat 294 296 . . . Note=2 O88339 UniProtKB Repeat 306 308 . . . Note=3 O88339 UniProtKB Repeat 319 321 . . . Note=4 O88339 UniProtKB Repeat 332 334 . . . Note=5 O88339 UniProtKB Repeat 349 351 . . . Note=6 O88339 UniProtKB Repeat 367 369 . . . Note=7 O88339 UniProtKB Repeat 377 379 . . . Note=8 O88339 UniProtKB Repeat 501 503 . . . Note=1 O88339 UniProtKB Repeat 517 519 . . . Note=2 O88339 UniProtKB Repeat 571 573 . . . Note=3 O88339 UniProtKB Region 149 186 . . . Note=Disordered;Ontology_term=ECO:0000256;evidence=ECO:0000256|SAM:MobiDB-lite O88339 UniProtKB Region 264 283 . . . Note=Disordered;Ontology_term=ECO:0000256;evidence=ECO:0000256|SAM:MobiDB-lite O88339 UniProtKB Region 274 379 . . . Note=8 X 3 AA repeats of D-P-W O88339 UniProtKB Region 293 575 . . . Note=Disordered;Ontology_term=ECO:0000256;evidence=ECO:0000256|SAM:MobiDB-lite O88339 UniProtKB Region 501 573 . . . Note=3 X 3 AA repeats of N-P-F O88339 UniProtKB Motif 401 410 . . . Note=[DE]-X(1%2C2)-F-X-X-[FL]-X-X-X-R motif O88339 UniProtKB Compositional bias 455 469 . . . Note=Pro residues;Ontology_term=ECO:0000256;evidence=ECO:0000256|SAM:MobiDB-lite O88339 UniProtKB Compositional bias 510 533 . . . Note=Polar residues;Ontology_term=ECO:0000256;evidence=ECO:0000256|SAM:MobiDB-lite O88339 UniProtKB Compositional bias 537 575 . . . Note=Pro residues;Ontology_term=ECO:0000256;evidence=ECO:0000256|SAM:MobiDB-lite O88339 UniProtKB Binding site 8 8 . . . . O88339 UniProtKB Binding site 11 11 . . . . O88339 UniProtKB Binding site 25 25 . . . . O88339 UniProtKB Binding site 30 30 . . . . O88339 UniProtKB Binding site 63 63 . . . . O88339 UniProtKB Binding site 73 73 . . . . O88339 UniProtKB Modified residue 382 382 . . . Note=Phosphoserine;Ontology_term=ECO:0000250;evidence=ECO:0000250|UniProtKB:Q9Y6I3 O88339 UniProtKB Modified residue 418 418 . . . Note=Phosphoserine;Ontology_term=ECO:0000250;evidence=ECO:0000250|UniProtKB:Q9Y6I3 O88339 UniProtKB Modified residue 419 419 . . . Note=Phosphoserine;Ontology_term=ECO:0000250;evidence=ECO:0000250|UniProtKB:Q9Y6I3 O88339 UniProtKB Modified residue 420 420 . . . Note=Phosphothreonine;Ontology_term=ECO:0000250;evidence=ECO:0000250|UniProtKB:Q80VP1 O88339 UniProtKB Modified residue 434 434 . . . Note=Phosphoserine;Ontology_term=ECO:0000250;evidence=ECO:0000250|UniProtKB:Q9Y6I3 O88339 UniProtKB Modified residue 446 446 . . . Note=Phosphoserine;Ontology_term=ECO:0000250;evidence=ECO:0000250|UniProtKB:Q9Y6I3 O88339 UniProtKB Modified residue 453 453 . . . Note=Phosphoserine;Ontology_term=ECO:0007744;evidence=ECO:0007744|PubMed:22673903;Dbxref=PMID:22673903 O88339 UniProtKB Modified residue 459 459 . . . Note=Phosphothreonine;Ontology_term=ECO:0000250;evidence=ECO:0000250|UniProtKB:Q9Y6I3 O88339 UniProtKB Modified residue 463 463 . . . Note=Phosphothreonine;Ontology_term=ECO:0000250;evidence=ECO:0000250|UniProtKB:Q9Y6I3 O88339 UniProtKB Modified residue 469 469 . . . Note=Phosphothreonine;Ontology_term=ECO:0007744;evidence=ECO:0007744|PubMed:22673903;Dbxref=PMID:22673903 O88339 UniProtKB Modified residue 472 472 . . . Note=Phosphoserine;Ontology_term=ECO:0000250;evidence=ECO:0000250|UniProtKB:Q80VP1 O88339 UniProtKB Modified residue 493 493 . . . Note=Phosphothreonine;Ontology_term=ECO:0000250;evidence=ECO:0000250|UniProtKB:Q9Y6I3 O88339 UniProtKB Modified residue 533 533 . . . Note=Omega-N-methylarginine;Ontology_term=ECO:0000250;evidence=ECO:0000250|UniProtKB:Q80VP1 O88339 UniProtKB Mutagenesis 6 6 . . . Note=Reduces lipid binding. L->E%2CH%2CQ;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:12353027;Dbxref=PMID:12353027 O88339 UniProtKB Mutagenesis 8 8 . . . Note=Strongly reduces lipid binding. R->A;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:11161217;Dbxref=PMID:11161217 O88339 UniProtKB Mutagenesis 63 63 . . . Note=Strongly reduces lipid binding. Abolishes lipid binding%3B when associated with L-73. R->L;Ontology_term=ECO:0000269,ECO:0000269;evidence=ECO:0000269|PubMed:11161217,ECO:0000269|PubMed:12353027;Dbxref=PMID:11161217,PMID:12353027 O88339 UniProtKB Mutagenesis 72 72 . . . Note=Abolishes ZNF145 binding. R->A;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:11161217;Dbxref=PMID:11161217 O88339 UniProtKB Mutagenesis 73 73 . . . Note=Abolishes lipid binding%3B when associated with L-63. H->L;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:12353027;Dbxref=PMID:12353027 O88339 UniProtKB Mutagenesis 76 76 . . . Note=Strongly reduces lipid binding. K->A;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:11161217;Dbxref=PMID:11161217 O88339 UniProtKB Mutagenesis 190 190 . . . Note=Abolishes mono-ubiquitination. L->A;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:11919637;Dbxref=PMID:11919637 O88339 UniProtKB Mutagenesis 257 259 . . . Note=Strongly reduces clathrin binding. LMD->AAA;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:10692452;Dbxref=PMID:10692452 O88339 UniProtKB Mutagenesis 260 263 . . . Note=Strongly reduces clathrin binding. LADV->AAAA;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:10692452;Dbxref=PMID:10692452 O88339 UniProtKB Helix 2 15 . . . Ontology_term=ECO:0007829;evidence=ECO:0007829|PDB:1H0A O88339 UniProtKB Helix 19 27 . . . Ontology_term=ECO:0007829;evidence=ECO:0007829|PDB:1EYH O88339 UniProtKB Beta strand 30 33 . . . Ontology_term=ECO:0007829;evidence=ECO:0007829|PDB:1EYH O88339 UniProtKB Helix 37 46 . . . Ontology_term=ECO:0007829;evidence=ECO:0007829|PDB:1EYH O88339 UniProtKB Helix 50 64 . . . Ontology_term=ECO:0007829;evidence=ECO:0007829|PDB:1EYH O88339 UniProtKB Helix 68 70 . . . Ontology_term=ECO:0007829;evidence=ECO:0007829|PDB:1EYH O88339 UniProtKB Helix 71 87 . . . Ontology_term=ECO:0007829;evidence=ECO:0007829|PDB:1EYH O88339 UniProtKB Helix 90 98 . . . Ontology_term=ECO:0007829;evidence=ECO:0007829|PDB:1EYH O88339 UniProtKB Helix 100 104 . . . Ontology_term=ECO:0007829;evidence=ECO:0007829|PDB:1EYH O88339 UniProtKB Helix 105 108 . . . Ontology_term=ECO:0007829;evidence=ECO:0007829|PDB:1EYH O88339 UniProtKB Helix 120 135 . . . Ontology_term=ECO:0007829;evidence=ECO:0007829|PDB:1EYH O88339 UniProtKB Helix 137 155 . . . Ontology_term=ECO:0007829;evidence=ECO:0007829|PDB:1EYH