##gff-version 3 Q07014 UniProtKB Initiator methionine 1 1 . . . Note=Removed;Ontology_term=ECO:0000250;evidence=ECO:0000250|UniProtKB:P07948 Q07014 UniProtKB Chain 2 512 . . . ID=PRO_0000088131;Note=Tyrosine-protein kinase Lyn Q07014 UniProtKB Domain 63 123 . . . Note=SH3;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00192 Q07014 UniProtKB Domain 129 226 . . . Note=SH2;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00191 Q07014 UniProtKB Domain 247 501 . . . Note=Protein kinase;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00159 Q07014 UniProtKB Region 1 50 . . . Note=Disordered;Ontology_term=ECO:0000256;evidence=ECO:0000256|SAM:MobiDB-lite Q07014 UniProtKB Compositional bias 1 16 . . . Note=Basic and acidic residues;Ontology_term=ECO:0000256;evidence=ECO:0000256|SAM:MobiDB-lite Q07014 UniProtKB Compositional bias 23 48 . . . Note=Polar residues;Ontology_term=ECO:0000256;evidence=ECO:0000256|SAM:MobiDB-lite Q07014 UniProtKB Active site 367 367 . . . Note=Proton acceptor;Ontology_term=ECO:0000255,ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00159,ECO:0000255|PROSITE-ProRule:PRU10028 Q07014 UniProtKB Binding site 253 261 . . . Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00159 Q07014 UniProtKB Binding site 275 275 . . . Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00159 Q07014 UniProtKB Modified residue 193 193 . . . Note=Phosphotyrosine;Ontology_term=ECO:0000250;evidence=ECO:0000250|UniProtKB:P07948 Q07014 UniProtKB Modified residue 228 228 . . . Note=Phosphoserine;Ontology_term=ECO:0000250;evidence=ECO:0000250|UniProtKB:P07948 Q07014 UniProtKB Modified residue 306 306 . . . Note=Phosphotyrosine;Ontology_term=ECO:0000250;evidence=ECO:0000250|UniProtKB:P07948 Q07014 UniProtKB Modified residue 316 316 . . . Note=Phosphotyrosine;Ontology_term=ECO:0007744;evidence=ECO:0007744|PubMed:22673903;Dbxref=PMID:22673903 Q07014 UniProtKB Modified residue 397 397 . . . Note=Phosphotyrosine%3B by autocatalysis;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:9477973;Dbxref=PMID:9477973 Q07014 UniProtKB Modified residue 460 460 . . . Note=Phosphotyrosine;Ontology_term=ECO:0000250;evidence=ECO:0000250|UniProtKB:P07948 Q07014 UniProtKB Modified residue 473 473 . . . Note=Phosphotyrosine;Ontology_term=ECO:0000250;evidence=ECO:0000250|UniProtKB:P07948 Q07014 UniProtKB Modified residue 508 508 . . . Note=Phosphotyrosine%3B by autocatalysis%2C CSK and MATK;Ontology_term=ECO:0000269,ECO:0007744;evidence=ECO:0000269|PubMed:9477973,ECO:0007744|PubMed:22673903;Dbxref=PMID:22673903,PMID:9477973 Q07014 UniProtKB Lipidation 2 2 . . . Note=N-myristoyl glycine;Ontology_term=ECO:0000250;evidence=ECO:0000250|UniProtKB:P07948 Q07014 UniProtKB Lipidation 3 3 . . . Note=S-palmitoyl cysteine;Ontology_term=ECO:0000250;evidence=ECO:0000250 Q07014 UniProtKB Alternative sequence 25 45 . . . ID=VSP_005004;Note=In isoform LYNB. Missing;Ontology_term=ECO:0000305;evidence=ECO:0000305 Q07014 UniProtKB Sequence conflict 231 231 . . . Note=P->L;Ontology_term=ECO:0000305;evidence=ECO:0000305 Q07014 UniProtKB Sequence conflict 308 308 . . . Note=V->A;Ontology_term=ECO:0000305;evidence=ECO:0000305 Q07014 UniProtKB Sequence conflict 419 419 . . . Note=C->Y;Ontology_term=ECO:0000305;evidence=ECO:0000305