##gff-version 3
O60927	UniProtKB	Initiator methionine	1	1	.	.	.	Note=Removed;Ontology_term=ECO:0007744;evidence=ECO:0007744|PubMed:22814378;Dbxref=PMID:22814378	
O60927	UniProtKB	Chain	2	126	.	.	.	ID=PRO_0000239619;Note=E3 ubiquitin-protein ligase PPP1R11	
O60927	UniProtKB	Region	1	25	.	.	.	Note=Disordered;Ontology_term=ECO:0000256;evidence=ECO:0000256|SAM:MobiDB-lite	
O60927	UniProtKB	Region	52	62	.	.	.	Note=Atypical RING finger domain 1;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:27805901;Dbxref=PMID:27805901	
O60927	UniProtKB	Region	70	126	.	.	.	Note=Disordered;Ontology_term=ECO:0000256;evidence=ECO:0000256|SAM:MobiDB-lite	
O60927	UniProtKB	Region	85	94	.	.	.	Note=Atypical RING finger domain 2;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:27805901;Dbxref=PMID:27805901	
O60927	UniProtKB	Compositional bias	9	25	.	.	.	Note=Polar residues;Ontology_term=ECO:0000256;evidence=ECO:0000256|SAM:MobiDB-lite	
O60927	UniProtKB	Compositional bias	106	126	.	.	.	Note=Pro residues;Ontology_term=ECO:0000256;evidence=ECO:0000256|SAM:MobiDB-lite	
O60927	UniProtKB	Modified residue	2	2	.	.	.	Note=N-acetylalanine;Ontology_term=ECO:0007744;evidence=ECO:0007744|PubMed:22814378;Dbxref=PMID:22814378	
O60927	UniProtKB	Modified residue	73	73	.	.	.	Note=Phosphoserine;Ontology_term=ECO:0007744;evidence=ECO:0007744|PubMed:18669648;Dbxref=PMID:18669648	
O60927	UniProtKB	Modified residue	74	74	.	.	.	Note=Phosphoserine;Ontology_term=ECO:0007744;evidence=ECO:0007744|PubMed:18669648;Dbxref=PMID:18669648	
O60927	UniProtKB	Modified residue	75	75	.	.	.	Note=Phosphothreonine;Ontology_term=ECO:0007744;evidence=ECO:0007744|PubMed:18669648;Dbxref=PMID:18669648	
O60927	UniProtKB	Modified residue	77	77	.	.	.	Note=Phosphoserine;Ontology_term=ECO:0007744;evidence=ECO:0007744|PubMed:18669648;Dbxref=PMID:18669648	
O60927	UniProtKB	Modified residue	109	109	.	.	.	Note=Phosphothreonine;Ontology_term=ECO:0007744;evidence=ECO:0007744|PubMed:18669648;Dbxref=PMID:18669648	
O60927	UniProtKB	Mutagenesis	52	52	.	.	.	Note=Loss of function in inducing TLR2 degradation. H->A;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:27805901;Dbxref=PMID:27805901	
O60927	UniProtKB	Mutagenesis	60	62	.	.	.	Note=Loss of function in inducing TLR2 degradation. CCC->SSS;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:27805901;Dbxref=PMID:27805901	
O60927	UniProtKB	Mutagenesis	85	85	.	.	.	Note=Loss of function in inducing TLR2 degradation. C->S;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:27805901;Dbxref=PMID:27805901	
O60927	UniProtKB	Mutagenesis	87	87	.	.	.	Note=Loss of function in inducing TLR2 degradation. H->A;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:27805901;Dbxref=PMID:27805901	
O60927	UniProtKB	Mutagenesis	89	90	.	.	.	Note=Loss of function in inducing TLR2 degradation. HC->AS;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:27805901;Dbxref=PMID:27805901	
O60927	UniProtKB	Mutagenesis	94	94	.	.	.	Note=Loss of function in inducing TLR2 degradation. H->A;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:27805901;Dbxref=PMID:27805901	
O60927	UniProtKB	Turn	51	54	.	.	.	Ontology_term=ECO:0007829;evidence=ECO:0007829|PDB:8DWK	
O60927	UniProtKB	Beta strand	57	59	.	.	.	Ontology_term=ECO:0007829;evidence=ECO:0007829|PDB:8DWL