##gff-version 3
P49710	UniProtKB	Chain	1	486	.	.	.	ID=PRO_0000083922;Note=Hematopoietic lineage cell-specific protein	
P49710	UniProtKB	Repeat	79	115	.	.	.	Note=Cortactin 1	
P49710	UniProtKB	Repeat	116	152	.	.	.	Note=Cortactin 2	
P49710	UniProtKB	Repeat	153	189	.	.	.	Note=Cortactin 3	
P49710	UniProtKB	Repeat	190	212	.	.	.	Note=Cortactin 4%3B truncated	
P49710	UniProtKB	Domain	429	486	.	.	.	Note=SH3;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00192	
P49710	UniProtKB	Region	27	66	.	.	.	Note=Involved in HAX-1 binding;Ontology_term=ECO:0000250;evidence=ECO:0000250	
P49710	UniProtKB	Region	226	430	.	.	.	Note=Disordered;Ontology_term=ECO:0000256;evidence=ECO:0000256|SAM:MobiDB-lite	
P49710	UniProtKB	Compositional bias	241	274	.	.	.	Note=Basic and acidic residues;Ontology_term=ECO:0000256;evidence=ECO:0000256|SAM:MobiDB-lite	
P49710	UniProtKB	Compositional bias	366	411	.	.	.	Note=Acidic residues;Ontology_term=ECO:0000256;evidence=ECO:0000256|SAM:MobiDB-lite	
P49710	UniProtKB	Modified residue	41	41	.	.	.	Note=N6-acetyllysine;Ontology_term=ECO:0000250;evidence=ECO:0000250|UniProtKB:P14317	
P49710	UniProtKB	Modified residue	123	123	.	.	.	Note=N6-acetyllysine;Ontology_term=ECO:0000250;evidence=ECO:0000250|UniProtKB:P14317	
P49710	UniProtKB	Modified residue	140	140	.	.	.	Note=Phosphotyrosine;Ontology_term=ECO:0007744;evidence=ECO:0007744|PubMed:17947660;Dbxref=PMID:17947660	
P49710	UniProtKB	Modified residue	192	192	.	.	.	Note=N6-acetyllysine;Ontology_term=ECO:0000250;evidence=ECO:0000250|UniProtKB:P14317	
P49710	UniProtKB	Modified residue	198	198	.	.	.	Note=Phosphotyrosine;Ontology_term=ECO:0000250;evidence=ECO:0000250|UniProtKB:P14317	
P49710	UniProtKB	Modified residue	222	222	.	.	.	Note=Phosphotyrosine%3B by FGR;Ontology_term=ECO:0000250;evidence=ECO:0000250|UniProtKB:P14317	
P49710	UniProtKB	Modified residue	241	241	.	.	.	Note=N6-acetyllysine;Ontology_term=ECO:0000250;evidence=ECO:0000250|UniProtKB:P14317	
P49710	UniProtKB	Modified residue	275	275	.	.	.	Note=Phosphoserine;Ontology_term=ECO:0000250;evidence=ECO:0000250|UniProtKB:P14317	
P49710	UniProtKB	Modified residue	330	330	.	.	.	Note=Phosphothreonine;Ontology_term=ECO:0007744;evidence=ECO:0007744|PubMed:21183079;Dbxref=PMID:21183079	
P49710	UniProtKB	Modified residue	333	333	.	.	.	Note=Phosphoserine;Ontology_term=ECO:0007744;evidence=ECO:0007744|PubMed:21183079;Dbxref=PMID:21183079	
P49710	UniProtKB	Modified residue	388	388	.	.	.	Note=Phosphotyrosine%3B by SYK and FES;Ontology_term=ECO:0000305;evidence=ECO:0000305|PubMed:19001085;Dbxref=PMID:19001085	
P49710	UniProtKB	Modified residue	405	405	.	.	.	Note=Phosphotyrosine%3B by SYK and FES;Ontology_term=ECO:0000305;evidence=ECO:0000305|PubMed:19001085;Dbxref=PMID:19001085	
P49710	UniProtKB	Mutagenesis	388	388	.	.	.	Note=Strongly reduces phosphorylation by FES. Abolishes phosphorylation by FES%3B when associated with F-405. Y->F;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:19001085;Dbxref=PMID:19001085	
P49710	UniProtKB	Mutagenesis	405	405	.	.	.	Note=Minor effect on phosphorylation by FES. Abolishes phosphorylation by FES%3B when associated with F-388. Y->F;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:19001085;Dbxref=PMID:19001085	
P49710	UniProtKB	Sequence conflict	86	86	.	.	.	Note=R->Q;Ontology_term=ECO:0000305;evidence=ECO:0000305