##gff-version 3 P07948 UniProtKB Initiator methionine 1 1 . . . Note=Removed;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:25255805;Dbxref=PMID:25255805 P07948 UniProtKB Chain 2 512 . . . ID=PRO_0000088129;Note=Tyrosine-protein kinase Lyn P07948 UniProtKB Domain 63 123 . . . Note=SH3;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00192 P07948 UniProtKB Domain 129 226 . . . Note=SH2;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00191 P07948 UniProtKB Domain 247 501 . . . Note=Protein kinase;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00159 P07948 UniProtKB Region 1 62 . . . Note=Disordered;Ontology_term=ECO:0000256;evidence=ECO:0000256|SAM:MobiDB-lite P07948 UniProtKB Compositional bias 23 55 . . . Note=Polar residues;Ontology_term=ECO:0000256;evidence=ECO:0000256|SAM:MobiDB-lite P07948 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 P07948 UniProtKB Binding site 253 261 . . . Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00159 P07948 UniProtKB Binding site 275 275 . . . Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00159 P07948 UniProtKB Modified residue 11 11 . . . Note=Phosphoserine;Ontology_term=ECO:0007744,ECO:0007744,ECO:0007744,ECO:0007744,ECO:0007744;evidence=ECO:0007744|PubMed:18691976,ECO:0007744|PubMed:19369195,ECO:0007744|PubMed:21406692,ECO:0007744|PubMed:23186163,ECO:0007744|PubMed:24275569;Dbxref=PMID:18691976,PMID:19369195,PMID:21406692,PMID:23186163,PMID:24275569 P07948 UniProtKB Modified residue 13 13 . . . Note=Phosphoserine;Ontology_term=ECO:0007744,ECO:0007744,ECO:0007744,ECO:0007744,ECO:0007744,ECO:0007744;evidence=ECO:0007744|PubMed:18691976,ECO:0007744|PubMed:19369195,ECO:0007744|PubMed:20068231,ECO:0007744|PubMed:21406692,ECO:0007744|PubMed:23186163,ECO:0007744|PubMed:24275569;Dbxref=PMID:18691976,PMID:19369195,PMID:20068231,PMID:21406692,PMID:23186163,PMID:24275569 P07948 UniProtKB Modified residue 193 193 . . . Note=Phosphotyrosine;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:18577747;Dbxref=PMID:18577747 P07948 UniProtKB Modified residue 228 228 . . . Note=Phosphoserine;Ontology_term=ECO:0007744;evidence=ECO:0007744|PubMed:19369195;Dbxref=PMID:19369195 P07948 UniProtKB Modified residue 306 306 . . . Note=Phosphotyrosine;Ontology_term=ECO:0007744;evidence=ECO:0007744|PubMed:19369195;Dbxref=PMID:19369195 P07948 UniProtKB Modified residue 316 316 . . . Note=Phosphotyrosine;Ontology_term=ECO:0007744;evidence=ECO:0007744|PubMed:19369195;Dbxref=PMID:19369195 P07948 UniProtKB Modified residue 397 397 . . . Note=Phosphotyrosine%3B by autocatalysis;Ontology_term=ECO:0000269,ECO:0000269;evidence=ECO:0000269|PubMed:18070987,ECO:0000269|PubMed:7935444;Dbxref=PMID:18070987,PMID:7935444 P07948 UniProtKB Modified residue 460 460 . . . Note=Phosphotyrosine;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:18577747;Dbxref=PMID:18577747 P07948 UniProtKB Modified residue 473 473 . . . Note=Phosphotyrosine;Ontology_term=ECO:0007744,ECO:0007744;evidence=ECO:0007744|PubMed:18691976,ECO:0007744|PubMed:19369195;Dbxref=PMID:18691976,PMID:19369195 P07948 UniProtKB Modified residue 508 508 . . . Note=Phosphotyrosine%3B by autocatalysis%2C CSK and MATK;Ontology_term=ECO:0000269,ECO:0000269,ECO:0000269,ECO:0007744,ECO:0007744,ECO:0007744;evidence=ECO:0000269|PubMed:18070987,ECO:0000269|PubMed:7935444,ECO:0000269|PubMed:9171348,ECO:0007744|PubMed:15592455,ECO:0007744|PubMed:18691976,ECO:0007744|PubMed:19369195;Dbxref=PMID:15592455,PMID:18070987,PMID:18691976,PMID:19369195,PMID:7935444,PMID:9171348 P07948 UniProtKB Lipidation 2 2 . . . Note=N-myristoyl glycine;Ontology_term=ECO:0000269,ECO:0000305;evidence=ECO:0000269|PubMed:25255805,ECO:0000305|PubMed:18817770;Dbxref=PMID:18817770,PMID:25255805 P07948 UniProtKB Lipidation 3 3 . . . Note=S-palmitoyl cysteine;Ontology_term=ECO:0000305;evidence=ECO:0000305|PubMed:18817770;Dbxref=PMID:18817770 P07948 UniProtKB Alternative sequence 23 43 . . . ID=VSP_005002;Note=In isoform 2. Missing;Ontology_term=ECO:0000303;evidence=ECO:0000303|PubMed:8125304;Dbxref=PMID:8125304 P07948 UniProtKB Natural variant 385 385 . . . ID=VAR_041737;Note=In a breast pleomorphic lobular carcinoma sample%3B somatic mutation. D->Y;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:17344846;Dbxref=PMID:17344846 P07948 UniProtKB Natural variant 507 512 . . . ID=VAR_088619;Note=In SAIDV%3B pathogenic%3B increased kinase activity due to loss of autoinhibition resulting in constitutive activation%3B loss of Y-508 phosphorylation%3B increased Y-397 phosphorylation. Missing;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:36932076;Dbxref=PMID:36932076 P07948 UniProtKB Natural variant 508 512 . . . ID=VAR_088620;Note=In SAIDV%3B pathogenic%3B increased kinase activity due to loss of autoinhibition resulting in constitutive activation%3B loss of Y-508 phosphorylation%3B increased Y-397 phosphorylation. Missing;Ontology_term=ECO:0000269,ECO:0000269,ECO:0000269;evidence=ECO:0000269|PubMed:36122175,ECO:0000269|PubMed:36932076,ECO:0000269|Ref.67;Dbxref=PMID:36122175,PMID:36932076 P07948 UniProtKB Natural variant 508 508 . . . ID=VAR_088621;Note=In SAIDV%3B pathogenic%3B increased kinase activity due to loss of autoinhibition resulting in constitutive activation%3B loss of Y-508 phosphorylation%3B increased Y-397 phosphorylation. Y->F;Ontology_term=ECO:0000269,ECO:0000269,ECO:0000269;evidence=ECO:0000269|PubMed:16920712,ECO:0000269|PubMed:36122175,ECO:0000269|PubMed:36932076;Dbxref=PMID:16920712,PMID:36122175,PMID:36932076 P07948 UniProtKB Natural variant 508 508 . . . ID=VAR_088622;Note=In SAIDV%3B pathogenic%3B increased kinase activity due to loss of autoinhibition resulting in constitutive activation%3B loss of Y-508 phosphorylation%3B increased Y-397 phosphorylation. Y->H;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:36122175;Dbxref=PMID:36122175 P07948 UniProtKB Mutagenesis 2 2 . . . Note=Loss of localization to the cell membrane%3B when associated with A-3. G->A;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:18817770;Dbxref=PMID:18817770 P07948 UniProtKB Mutagenesis 3 3 . . . Note=Loss of localization to the cell membrane%3B when associated with A-2. C->A;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:18817770;Dbxref=PMID:18817770 P07948 UniProtKB Mutagenesis 275 275 . . . Note=Loss of activity and no effect on localization to the cell membrane. Abundant localization in the nucleus%3B when associated with A-2 and A-3. K->A;Ontology_term=ECO:0000269,ECO:0000269,ECO:0000269,ECO:0000269;evidence=ECO:0000269|PubMed:11435302,ECO:0000269|PubMed:11517336,ECO:0000269|PubMed:15173188,ECO:0000269|PubMed:18817770;Dbxref=PMID:11435302,PMID:11517336,PMID:15173188,PMID:18817770 P07948 UniProtKB Mutagenesis 275 275 . . . Note=Loss of kinase activity. K->L%2CR;Ontology_term=ECO:0000269,ECO:0000269,ECO:0000269,ECO:0000269;evidence=ECO:0000269|PubMed:11435302,ECO:0000269|PubMed:11517336,ECO:0000269|PubMed:15173188,ECO:0000269|PubMed:18817770;Dbxref=PMID:11435302,PMID:11517336,PMID:15173188,PMID:18817770 P07948 UniProtKB Mutagenesis 346 346 . . . Note=Impedes the trafficking from the Golgi apparatus toward the cell membrane%3B when associated with A-353%3B A-498 and A-499. D->A;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:15173188;Dbxref=PMID:15173188 P07948 UniProtKB Mutagenesis 353 353 . . . Note=Impedes the trafficking from the Golgi apparatus toward the cell membrane%3B when associated with A-346%3B A-498 and A-499. E->A;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:15173188;Dbxref=PMID:15173188 P07948 UniProtKB Mutagenesis 397 397 . . . Note=Strongly reduced kinase activity. Y->F;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:16920712;Dbxref=PMID:16920712 P07948 UniProtKB Mutagenesis 498 498 . . . Note=Impedes the trafficking from the Golgi apparatus toward the cell membrane%3B when associated with A-346%3B A-353 and A-499. D->A;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:15173188;Dbxref=PMID:15173188 P07948 UniProtKB Mutagenesis 499 499 . . . Note=Impedes the trafficking from the Golgi apparatus toward the cell membrane%3B when associated with A-346%3B A-353 and A-498. D->A;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:15173188;Dbxref=PMID:15173188 P07948 UniProtKB Beta strand 67 72 . . . Ontology_term=ECO:0007829;evidence=ECO:0007829|PDB:6NMW P07948 UniProtKB Beta strand 78 80 . . . Ontology_term=ECO:0007829;evidence=ECO:0007829|PDB:1W1F P07948 UniProtKB Beta strand 89 96 . . . Ontology_term=ECO:0007829;evidence=ECO:0007829|PDB:6NMW P07948 UniProtKB Beta strand 99 104 . . . Ontology_term=ECO:0007829;evidence=ECO:0007829|PDB:6NMW P07948 UniProtKB Turn 105 107 . . . Ontology_term=ECO:0007829;evidence=ECO:0007829|PDB:6NMW P07948 UniProtKB Beta strand 110 114 . . . Ontology_term=ECO:0007829;evidence=ECO:0007829|PDB:6NMW P07948 UniProtKB Helix 115 117 . . . Ontology_term=ECO:0007829;evidence=ECO:0007829|PDB:6NMW P07948 UniProtKB Beta strand 118 121 . . . Ontology_term=ECO:0007829;evidence=ECO:0007829|PDB:6NMW P07948 UniProtKB Helix 244 246 . . . Ontology_term=ECO:0007829;evidence=ECO:0007829|PDB:5XY1 P07948 UniProtKB Beta strand 247 255 . . . Ontology_term=ECO:0007829;evidence=ECO:0007829|PDB:5XY1 P07948 UniProtKB Beta strand 260 266 . . . Ontology_term=ECO:0007829;evidence=ECO:0007829|PDB:5XY1 P07948 UniProtKB Turn 267 269 . . . Ontology_term=ECO:0007829;evidence=ECO:0007829|PDB:5XY1 P07948 UniProtKB Beta strand 270 277 . . . Ontology_term=ECO:0007829;evidence=ECO:0007829|PDB:5XY1 P07948 UniProtKB Helix 284 296 . . . Ontology_term=ECO:0007829;evidence=ECO:0007829|PDB:5XY1 P07948 UniProtKB Beta strand 305 309 . . . Ontology_term=ECO:0007829;evidence=ECO:0007829|PDB:5XY1 P07948 UniProtKB Beta strand 311 320 . . . Ontology_term=ECO:0007829;evidence=ECO:0007829|PDB:5XY1 P07948 UniProtKB Helix 327 332 . . . Ontology_term=ECO:0007829;evidence=ECO:0007829|PDB:5XY1 P07948 UniProtKB Helix 334 338 . . . Ontology_term=ECO:0007829;evidence=ECO:0007829|PDB:5XY1 P07948 UniProtKB Helix 341 360 . . . Ontology_term=ECO:0007829;evidence=ECO:0007829|PDB:5XY1 P07948 UniProtKB Helix 370 372 . . . Ontology_term=ECO:0007829;evidence=ECO:0007829|PDB:5XY1 P07948 UniProtKB Beta strand 373 375 . . . Ontology_term=ECO:0007829;evidence=ECO:0007829|PDB:5XY1 P07948 UniProtKB Beta strand 381 383 . . . Ontology_term=ECO:0007829;evidence=ECO:0007829|PDB:5XY1 P07948 UniProtKB Helix 407 409 . . . Ontology_term=ECO:0007829;evidence=ECO:0007829|PDB:5XY1 P07948 UniProtKB Helix 412 417 . . . Ontology_term=ECO:0007829;evidence=ECO:0007829|PDB:5XY1 P07948 UniProtKB Helix 422 437 . . . Ontology_term=ECO:0007829;evidence=ECO:0007829|PDB:5XY1 P07948 UniProtKB Helix 449 457 . . . Ontology_term=ECO:0007829;evidence=ECO:0007829|PDB:5XY1 P07948 UniProtKB Beta strand 466 468 . . . Ontology_term=ECO:0007829;evidence=ECO:0007829|PDB:5XY1 P07948 UniProtKB Helix 470 479 . . . Ontology_term=ECO:0007829;evidence=ECO:0007829|PDB:5XY1 P07948 UniProtKB Helix 484 486 . . . Ontology_term=ECO:0007829;evidence=ECO:0007829|PDB:5XY1 P07948 UniProtKB Helix 490 501 . . . Ontology_term=ECO:0007829;evidence=ECO:0007829|PDB:5XY1