##gff-version 3
P10936	UniProtKB	Initiator methionine	1	1	.	.	.	Note=Removed;Ontology_term=ECO:0000250;evidence=ECO:0000250	
P10936	UniProtKB	Chain	2	537	.	.	.	ID=PRO_0000088184;Note=Tyrosine-protein kinase Yes	
P10936	UniProtKB	Domain	85	146	.	.	.	Note=SH3;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00192	
P10936	UniProtKB	Domain	152	249	.	.	.	Note=SH2;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00191	
P10936	UniProtKB	Domain	271	524	.	.	.	Note=Protein kinase;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00159	
P10936	UniProtKB	Region	1	60	.	.	.	Note=Disordered;Ontology_term=ECO:0000256;evidence=ECO:0000256|SAM:MobiDB-lite	
P10936	UniProtKB	Compositional bias	1	17	.	.	.	Note=Basic and acidic residues;Ontology_term=ECO:0000256;evidence=ECO:0000256|SAM:MobiDB-lite	
P10936	UniProtKB	Compositional bias	29	60	.	.	.	Note=Polar residues;Ontology_term=ECO:0000256;evidence=ECO:0000256|SAM:MobiDB-lite	
P10936	UniProtKB	Active site	390	390	.	.	.	Note=Proton acceptor;Ontology_term=ECO:0000255,ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00159,ECO:0000255|PROSITE-ProRule:PRU10028	
P10936	UniProtKB	Binding site	277	285	.	.	.	Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00159	
P10936	UniProtKB	Binding site	299	299	.	.	.	Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00159	
P10936	UniProtKB	Modified residue	420	420	.	.	.	Note=Phosphotyrosine%3B by autocatalysis;Ontology_term=ECO:0000250;evidence=ECO:0000250	
P10936	UniProtKB	Modified residue	531	531	.	.	.	Note=Phosphotyrosine%3B by CSK;Ontology_term=ECO:0000250;evidence=ECO:0000250	
P10936	UniProtKB	Lipidation	2	2	.	.	.	Note=N-myristoyl glycine;Ontology_term=ECO:0000250;evidence=ECO:0000250	
P10936	UniProtKB	Lipidation	3	3	.	.	.	Note=S-palmitoyl cysteine%3B in membrane form;Ontology_term=ECO:0000250;evidence=ECO:0000250