##gff-version 3
P11836	UniProtKB	Chain	1	297	.	.	.	ID=PRO_0000158627;Note=B-lymphocyte antigen CD20	
P11836	UniProtKB	Topological domain	1	56	.	.	.	Note=Cytoplasmic;Ontology_term=ECO:0000255;evidence=ECO:0000255	
P11836	UniProtKB	Transmembrane	57	78	.	.	.	Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255	
P11836	UniProtKB	Topological domain	79	84	.	.	.	Note=Extracellular;Ontology_term=ECO:0000255;evidence=ECO:0000255	
P11836	UniProtKB	Transmembrane	85	105	.	.	.	Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255	
P11836	UniProtKB	Topological domain	106	120	.	.	.	Note=Cytoplasmic;Ontology_term=ECO:0000255;evidence=ECO:0000255	
P11836	UniProtKB	Transmembrane	121	141	.	.	.	Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255	
P11836	UniProtKB	Topological domain	142	188	.	.	.	Note=Extracellular;Ontology_term=ECO:0000255;evidence=ECO:0000255	
P11836	UniProtKB	Transmembrane	189	209	.	.	.	Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255	
P11836	UniProtKB	Topological domain	210	297	.	.	.	Note=Cytoplasmic;Ontology_term=ECO:0000255;evidence=ECO:0000255	
P11836	UniProtKB	Region	74	80	.	.	.	Note=Epitope 1	
P11836	UniProtKB	Region	146	160	.	.	.	Note=Epitope 2	
P11836	UniProtKB	Region	168	175	.	.	.	Note=Epitope 3 (recognized by antibodies%2C including Rituximab)	
P11836	UniProtKB	Region	247	297	.	.	.	Note=Disordered;Ontology_term=ECO:0000256;evidence=ECO:0000256|SAM:MobiDB-lite	
P11836	UniProtKB	Compositional bias	264	280	.	.	.	Note=Acidic residues;Ontology_term=ECO:0000256;evidence=ECO:0000256|SAM:MobiDB-lite	
P11836	UniProtKB	Compositional bias	281	297	.	.	.	Note=Polar residues;Ontology_term=ECO:0000256;evidence=ECO:0000256|SAM:MobiDB-lite	
P11836	UniProtKB	Modified residue	36	36	.	.	.	Note=Phosphoserine;Ontology_term=ECO:0000250;evidence=ECO:0000250|UniProtKB:P19437	
P11836	UniProtKB	Modified residue	225	225	.	.	.	Note=Phosphoserine;Ontology_term=ECO:0000250;evidence=ECO:0000250|UniProtKB:P19437	
P11836	UniProtKB	Modified residue	239	239	.	.	.	Note=Phosphothreonine;Ontology_term=ECO:0000250;evidence=ECO:0000250|UniProtKB:P19437	
P11836	UniProtKB	Lipidation	111	111	.	.	.	Note=S-palmitoyl cysteine;Ontology_term=ECO:0000305;evidence=ECO:0000305|PubMed:22615937;Dbxref=PMID:22615937	
P11836	UniProtKB	Lipidation	220	220	.	.	.	Note=S-palmitoyl cysteine;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:22615937;Dbxref=PMID:22615937	
P11836	UniProtKB	Disulfide bond	167	183	.	.	.	Ontology_term=ECO:0000269,ECO:0000269,ECO:0000269;evidence=ECO:0000269|PubMed:17395584,ECO:0000269|PubMed:18346788,ECO:0000269|PubMed:21444918;Dbxref=PMID:17395584,PMID:18346788,PMID:21444918	
P11836	UniProtKB	Alternative sequence	38	204	.	.	.	ID=VSP_057058;Note=In isoform 2. Missing;Ontology_term=ECO:0000303;evidence=ECO:0000303|PubMed:14702039;Dbxref=PMID:14702039	
P11836	UniProtKB	Mutagenesis	159	159	.	.	.	Note=Abrogates recognition by some antibodies%3B when associated with D-163 and D-166. Slight decrease of rituximab binding%3B when associated with D-163 and D-166. T->K;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:16785532;Dbxref=PMID:16785532	
P11836	UniProtKB	Mutagenesis	163	163	.	.	.	Note=Decreased binding of some antibodies. No effect on rituximab binding. N->D;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:16785532;Dbxref=PMID:16785532	
P11836	UniProtKB	Mutagenesis	166	166	.	.	.	Note=Decreased binding of some antibodies. No effect on rituximab binding. N->D;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:16785532;Dbxref=PMID:16785532	
P11836	UniProtKB	Mutagenesis	170	170	.	.	.	Note=Abrogates recognition by therapeutic antibodies%2C including rituximab%3B when associated with S-172. A->S;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:16785532;Dbxref=PMID:16785532	
P11836	UniProtKB	Mutagenesis	172	172	.	.	.	Note=Marked reduction in rituximab binding. Abrogates recognition by antibodies%2C including rituximab%3B when associated with S-170. P->S;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:16785532;Dbxref=PMID:16785532	
P11836	UniProtKB	Sequence conflict	13	13	.	.	.	Note=P->L;Ontology_term=ECO:0000305;evidence=ECO:0000305	
P11836	UniProtKB	Sequence conflict	71	71	.	.	.	Note=M->I;Ontology_term=ECO:0000305;evidence=ECO:0000305	
P11836	UniProtKB	Helix	48	70	.	.	.	Ontology_term=ECO:0007829;evidence=ECO:0007829|PDB:6VJA	
P11836	UniProtKB	Helix	80	83	.	.	.	Ontology_term=ECO:0007829;evidence=ECO:0007829|PDB:6VJA	
P11836	UniProtKB	Helix	86	96	.	.	.	Ontology_term=ECO:0007829;evidence=ECO:0007829|PDB:6VJA	
P11836	UniProtKB	Helix	97	101	.	.	.	Ontology_term=ECO:0007829;evidence=ECO:0007829|PDB:6VJA	
P11836	UniProtKB	Beta strand	107	109	.	.	.	Ontology_term=ECO:0007829;evidence=ECO:0007829|PDB:6VJA	
P11836	UniProtKB	Helix	115	142	.	.	.	Ontology_term=ECO:0007829;evidence=ECO:0007829|PDB:6VJA	
P11836	UniProtKB	Helix	153	156	.	.	.	Ontology_term=ECO:0007829;evidence=ECO:0007829|PDB:6VJA	
P11836	UniProtKB	Helix	172	174	.	.	.	Ontology_term=ECO:0007829;evidence=ECO:0007829|PDB:3PP4	
P11836	UniProtKB	Helix	178	185	.	.	.	Ontology_term=ECO:0007829;evidence=ECO:0007829|PDB:3PP4	
P11836	UniProtKB	Turn	206	209	.	.	.	Ontology_term=ECO:0007829;evidence=ECO:0007829|PDB:6VJA