##gff-version 3
Q28923	UniProtKB	Initiator methionine	1	1	.	.	.	Note=Removed	
Q28923	UniProtKB	Chain	2	539	.	.	.	ID=PRO_0000088180;Note=Tyrosine-protein kinase Yes	
Q28923	UniProtKB	Domain	87	148	.	.	.	Note=SH3;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00192	
Q28923	UniProtKB	Domain	154	251	.	.	.	Note=SH2;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00191	
Q28923	UniProtKB	Domain	273	526	.	.	.	Note=Protein kinase;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00159	
Q28923	UniProtKB	Active site	392	392	.	.	.	Note=Proton acceptor;Ontology_term=ECO:0000255,ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00159,ECO:0000255|PROSITE-ProRule:PRU10028	
Q28923	UniProtKB	Binding site	279	287	.	.	.	Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00159	
Q28923	UniProtKB	Binding site	301	301	.	.	.	Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00159	
Q28923	UniProtKB	Modified residue	19	19	.	.	.	Note=Phosphothreonine;Ontology_term=ECO:0000250;evidence=ECO:0000250|UniProtKB:P07947	
Q28923	UniProtKB	Modified residue	28	28	.	.	.	Note=Phosphotyrosine;Ontology_term=ECO:0000250;evidence=ECO:0000250|UniProtKB:Q04736	
Q28923	UniProtKB	Modified residue	332	332	.	.	.	Note=Phosphotyrosine;Ontology_term=ECO:0000250;evidence=ECO:0000250|UniProtKB:P07947	
Q28923	UniProtKB	Modified residue	341	341	.	.	.	Note=Phosphotyrosine;Ontology_term=ECO:0000250;evidence=ECO:0000250|UniProtKB:P07947	
Q28923	UniProtKB	Modified residue	422	422	.	.	.	Note=Phosphotyrosine%3B by autocatalysis;Ontology_term=ECO:0000250;evidence=ECO:0000250|UniProtKB:P07947	
Q28923	UniProtKB	Modified residue	533	533	.	.	.	Note=Phosphotyrosine%3B by CSK;Ontology_term=ECO:0000250;evidence=ECO:0000250|UniProtKB:P07947	
Q28923	UniProtKB	Lipidation	2	2	.	.	.	Note=N-myristoyl glycine;Ontology_term=ECO:0000250;evidence=ECO:0000250	
Q28923	UniProtKB	Lipidation	3	3	.	.	.	Note=S-palmitoyl cysteine%3B in membrane form;Ontology_term=ECO:0000250;evidence=ECO:0000250