##gff-version 3
P39929	UniProtKB	Chain	1	240	.	.	.	ID=PRO_0000211446;Note=Vacuolar-sorting protein SNF7	
P39929	UniProtKB	Region	193	240	.	.	.	Note=Disordered;Ontology_term=ECO:0000256;evidence=ECO:0000256|SAM:MobiDB-lite	
P39929	UniProtKB	Compositional bias	193	210	.	.	.	Note=Polar residues;Ontology_term=ECO:0000256;evidence=ECO:0000256|SAM:MobiDB-lite	
P39929	UniProtKB	Compositional bias	216	230	.	.	.	Note=Acidic residues;Ontology_term=ECO:0000256;evidence=ECO:0000256|SAM:MobiDB-lite	
P39929	UniProtKB	Modified residue	72	72	.	.	.	Note=Phosphothreonine;Ontology_term=ECO:0007744,ECO:0007744;evidence=ECO:0007744|PubMed:17287358,ECO:0007744|PubMed:17330950;Dbxref=PMID:17287358,PMID:17330950	
P39929	UniProtKB	Modified residue	119	119	.	.	.	Note=Phosphoserine;Ontology_term=ECO:0007744;evidence=ECO:0007744|PubMed:18407956;Dbxref=PMID:18407956	
P39929	UniProtKB	Modified residue	193	193	.	.	.	Note=Phosphoserine;Ontology_term=ECO:0007744;evidence=ECO:0007744|PubMed:18407956;Dbxref=PMID:18407956	
P39929	UniProtKB	Cross-link	229	229	.	.	.	Note=Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin);Ontology_term=ECO:0007744;evidence=ECO:0007744|PubMed:22106047;Dbxref=PMID:22106047	
P39929	UniProtKB	Mutagenesis	2	2	.	.	.	Note=Impairs binding to membrane. W->E;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:24139821;Dbxref=PMID:24139821	
P39929	UniProtKB	Mutagenesis	6	6	.	.	.	Note=Impairs binding to membrane. F->E;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:24139821;Dbxref=PMID:24139821	
P39929	UniProtKB	Mutagenesis	8	8	.	.	.	Note=Impairs binding to membrane. W->E;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:24139821;Dbxref=PMID:24139821	
P39929	UniProtKB	Mutagenesis	25	25	.	.	.	Note=Leads to severe sorting defects%3B when associated with E-29 and E-36. R->E;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:26670543;Dbxref=PMID:26670543	
P39929	UniProtKB	Mutagenesis	29	29	.	.	.	Note=Leads to severe sorting defects%3B when associated with E-25 and E-36. H->E;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:26670543;Dbxref=PMID:26670543	
P39929	UniProtKB	Mutagenesis	36	36	.	.	.	Note=Leads to severe sorting defects%3B when associated with E-25 and E-29. K->E;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:26670543;Dbxref=PMID:26670543	
P39929	UniProtKB	Mutagenesis	52	52	.	.	.	Note=Impairs the formation of protofilaments%3B when associated with K-90. Also impairs the formation of protofilaments%3B when associated with E-94. Also impairs the formation of protofilaments%3B when associated with E-107. Also impairs the formation of protofilaments%3B when associated with E-114. R->E;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:26670543;Dbxref=PMID:26670543	
P39929	UniProtKB	Mutagenesis	83	83	.	.	.	Note=Leads to severe sorting defects. T->E;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:26670543;Dbxref=PMID:26670543	
P39929	UniProtKB	Mutagenesis	87	87	.	.	.	Note=Leads to severe sorting defects. M->E;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:26670543;Dbxref=PMID:26670543	
P39929	UniProtKB	Mutagenesis	90	90	.	.	.	Note=Leads to severe sorting defects. Impairs the formation of protofilaments%3B when associated with E-52. Q->K;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:26670543;Dbxref=PMID:26670543	
P39929	UniProtKB	Mutagenesis	94	94	.	.	.	Note=Leads to severe sorting defects. Impairs the formation of protofilaments%3B when associated with E-52. I->E;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:26670543;Dbxref=PMID:26670543	
P39929	UniProtKB	Mutagenesis	95	95	.	.	.	Note=Leads to severe sorting defects%3B when associated with K-102 and K-109. E->K;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:26670543;Dbxref=PMID:26670543	
P39929	UniProtKB	Mutagenesis	97	97	.	.	.	Note=Leads to severe sorting defects. A->K;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:26670543;Dbxref=PMID:26670543	
P39929	UniProtKB	Mutagenesis	99	99	.	.	.	Note=Leads to severe sorting defects. L->K;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:26670543;Dbxref=PMID:26670543	
P39929	UniProtKB	Mutagenesis	101	101	.	.	.	Note=Leads to severe sorting defects. L->E;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:26670543;Dbxref=PMID:26670543	
P39929	UniProtKB	Mutagenesis	102	102	.	.	.	Note=Leads to severe sorting defects%3B when associated with K-95 and K-109. E->K;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:26670543;Dbxref=PMID:26670543	
P39929	UniProtKB	Mutagenesis	103	103	.	.	.	Note=Leads to severe sorting defects. T->E;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:26670543;Dbxref=PMID:26670543	
P39929	UniProtKB	Mutagenesis	104	104	.	.	.	Note=Leads to severe sorting defects. M->E;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:26670543;Dbxref=PMID:26670543	
P39929	UniProtKB	Mutagenesis	107	107	.	.	.	Note=Leads to severe sorting defects. Impairs the formation of protofilaments%3B when associated with E-52. M->E;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:26670543;Dbxref=PMID:26670543	
P39929	UniProtKB	Mutagenesis	109	109	.	.	.	Note=Leads to severe sorting defects%3B when associated with K-95 and K-102. E->K;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:26670543;Dbxref=PMID:26670543	
P39929	UniProtKB	Mutagenesis	114	114	.	.	.	Note=Leads to severe sorting defects. Impairs the formation of protofilaments%3B when associated with E-52. M->E;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:26670543;Dbxref=PMID:26670543	
P39929	UniProtKB	Mutagenesis	117	117	.	.	.	Note=Leads to severe sorting defects. I->E;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:26670543;Dbxref=PMID:26670543	
P39929	UniProtKB	Mutagenesis	121	121	.	.	.	Note=Leads to severe sorting defects. L->D;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:26670543;Dbxref=PMID:26670543	
P39929	UniProtKB	Sequence conflict	173	173	.	.	.	Note=E->G;Ontology_term=ECO:0000305;evidence=ECO:0000305	
P39929	UniProtKB	Helix	19	56	.	.	.	Ontology_term=ECO:0007829;evidence=ECO:0007829|PDB:5FD9	
P39929	UniProtKB	Helix	60	118	.	.	.	Ontology_term=ECO:0007829;evidence=ECO:0007829|PDB:5FD9	
P39929	UniProtKB	Turn	120	122	.	.	.	Ontology_term=ECO:0007829;evidence=ECO:0007829|PDB:5FD7	
P39929	UniProtKB	Helix	127	138	.	.	.	Ontology_term=ECO:0007829;evidence=ECO:0007829|PDB:5FD9	
P39929	UniProtKB	Turn	139	141	.	.	.	Ontology_term=ECO:0007829;evidence=ECO:0007829|PDB:5FD9