##gff-version 3 P04412 UniProtKB Signal peptide 1 30 . . . Ontology_term=ECO:0000255;evidence=ECO:0000255 P04412 UniProtKB Chain 31 1426 . . . ID=PRO_0000016676;Note=Epidermal growth factor receptor P04412 UniProtKB Topological domain 31 868 . . . Note=Extracellular;Ontology_term=ECO:0000255;evidence=ECO:0000255 P04412 UniProtKB Transmembrane 869 889 . . . Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255 P04412 UniProtKB Topological domain 890 1426 . . . Note=Cytoplasmic;Ontology_term=ECO:0000255;evidence=ECO:0000255 P04412 UniProtKB Domain 938 1198 . . . Note=Protein kinase;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00159 P04412 UniProtKB Region 1232 1297 . . . Note=Disordered;Ontology_term=ECO:0000256;evidence=ECO:0000256|SAM:MobiDB-lite P04412 UniProtKB Compositional bias 1279 1293 . . . Note=Basic and acidic residues;Ontology_term=ECO:0000256;evidence=ECO:0000256|SAM:MobiDB-lite P04412 UniProtKB Active site 1063 1063 . . . Note=Proton acceptor;Ontology_term=ECO:0000255,ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00159,ECO:0000255|PROSITE-ProRule:PRU10028 P04412 UniProtKB Binding site 944 952 . . . Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00159 P04412 UniProtKB Binding site 971 971 . . . Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00159 P04412 UniProtKB Modified residue 902 902 . . . Note=Phosphothreonine%3B by PKC;Ontology_term=ECO:0000250;evidence=ECO:0000250 P04412 UniProtKB Modified residue 1310 1310 . . . Note=Phosphotyrosine%3B by autocatalysis;Ontology_term=ECO:0000250;evidence=ECO:0000250 P04412 UniProtKB Glycosylation 128 128 . . . Note=N-linked (GlcNAc...) asparagine;Ontology_term=ECO:0007744;evidence=ECO:0007744|PDB:3LTF P04412 UniProtKB Glycosylation 241 241 . . . Note=N-linked (GlcNAc...) asparagine;Ontology_term=ECO:0000255;evidence=ECO:0000255 P04412 UniProtKB Glycosylation 419 419 . . . Note=N-linked (GlcNAc...) asparagine;Ontology_term=ECO:0000255;evidence=ECO:0000255 P04412 UniProtKB Glycosylation 443 443 . . . Note=N-linked (GlcNAc...) asparagine;Ontology_term=ECO:0007744,ECO:0007744;evidence=ECO:0007744|PDB:3I2T,ECO:0007744|PDB:3LTF P04412 UniProtKB Glycosylation 482 482 . . . Note=N-linked (GlcNAc...) asparagine;Ontology_term=ECO:0007744;evidence=ECO:0007744|PDB:3LTF P04412 UniProtKB Glycosylation 569 569 . . . Note=N-linked (GlcNAc...) asparagine;Ontology_term=ECO:0007744;evidence=ECO:0007744|PDB:3LTF P04412 UniProtKB Glycosylation 599 599 . . . Note=N-linked (GlcNAc...) asparagine;Ontology_term=ECO:0000255;evidence=ECO:0000255 P04412 UniProtKB Glycosylation 617 617 . . . Note=N-linked (GlcNAc...) asparagine;Ontology_term=ECO:0000255;evidence=ECO:0000255 P04412 UniProtKB Glycosylation 816 816 . . . Note=N-linked (GlcNAc...) asparagine;Ontology_term=ECO:0000255;evidence=ECO:0000255 P04412 UniProtKB Glycosylation 823 823 . . . Note=N-linked (GlcNAc...) asparagine;Ontology_term=ECO:0000255;evidence=ECO:0000255 P04412 UniProtKB Glycosylation 828 828 . . . Note=N-linked (GlcNAc...) asparagine;Ontology_term=ECO:0000255;evidence=ECO:0000255 P04412 UniProtKB Alternative sequence 1 101 . . . ID=VSP_002897;Note=In isoform Type II. MLLRRRNGPCPFPLLLLLLAHCICIWPASAARDRYARQNNRQRHQDIDRDRDRDRFLYRSSSAQNRQRGGANFALGLGANGVTIPTSLEDKNKNEFVKGKI->MMIISMWMSISRGLWDSSSILSVLLILACMASITTSSSVSNAGYVDNGNMKV;Ontology_term=ECO:0000305;evidence=ECO:0000305 P04412 UniProtKB Mutagenesis 101 101 . . . Note=Increased binding to spitz%3B when associated with A-101%3B A-358 and S-369. I->A;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:19718021;Dbxref=PMID:19718021 P04412 UniProtKB Mutagenesis 131 131 . . . Note=Increased binding to spitz%3B when associated with A-131%3B A-358 and S-369. Y->A;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:19718021;Dbxref=PMID:19718021 P04412 UniProtKB Mutagenesis 341 341 . . . Note=In dim-arm%3B Does not form dimers even in the presence of spitz%3B when associated with A-342%3B D-344%3B E-346%3B A-347 and D-348. Y->E;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:19718021;Dbxref=PMID:19718021 P04412 UniProtKB Mutagenesis 342 342 . . . Note=In dim-arm%3B Does not form dimers even in the presence of spitz%3B when associated with E-341%3B D-344%3B E-346%3B A-347 and D-348. N->A;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:19718021;Dbxref=PMID:19718021 P04412 UniProtKB Mutagenesis 344 344 . . . Note=>D: In dim-arm%3B Does not form dimers even in the presence of spitz%3B when associated with E-341%3B A-342%3B E-346%3B A-347 and D-348. T->D;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:19718021;Dbxref=PMID:19718021 P04412 UniProtKB Mutagenesis 346 346 . . . Note=In dim-arm%3B Does not form dimers even in the presence of spitz%3B when associated with E-341%3B A-342%3B D-344%3B A-347 and D-348. Y->E;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:19718021;Dbxref=PMID:19718021 P04412 UniProtKB Mutagenesis 347 347 . . . Note=In dim-arm%3B Does not form dimers even in the presence of Spitz%3B when associated with E-341%3B A-342%3B D-344%3B E-346 and D-348. V->A;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:19718021;Dbxref=PMID:19718021 P04412 UniProtKB Mutagenesis 348 348 . . . Note=In dim-arm%3B Does not form dimers even in the presence of spitz%3B when associated with E-341%3B A-342%3B D-344%3B E-346 and A-347. L->D;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:19718021;Dbxref=PMID:19718021 P04412 UniProtKB Mutagenesis 358 358 . . . Note=Reduced dissociation and increased binding to spitz%3B when associated with S-369. Increased binding to spitz%3B when associated with A-101%3B A-131 and S-369. Y->A;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:19718021;Dbxref=PMID:19718021 P04412 UniProtKB Mutagenesis 369 369 . . . Note=Reduced dissociation and increased binding to spitz%3B when associated with A-358. Increased binding to spitz%3B when associated with A-101%3B A-131 and A-358. H->S;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:19718021;Dbxref=PMID:19718021 P04412 UniProtKB Mutagenesis 592 1426 . . . Note=Slightly reduced affinity for spitz. Missing;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:19718021;Dbxref=PMID:19718021 P04412 UniProtKB Mutagenesis 646 646 . . . Note=In tether%3B No effect on binding to spitz%3B when associated with A-649 and A-658. D->A;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:19718021;Dbxref=PMID:19718021 P04412 UniProtKB Mutagenesis 649 649 . . . Note=In tether%3B No effect on binding to spitz%3B when associated with A-646 and A-658. H->A;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:19718021;Dbxref=PMID:19718021 P04412 UniProtKB Mutagenesis 658 658 . . . Note=In tether%3B No effect on binding to spitz%3B when associated with A-646 and A-649. K->A;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:19718021;Dbxref=PMID:19718021 P04412 UniProtKB Mutagenesis 688 1426 . . . Note=Forms dimers in presence of spitz. Forms weak dimers in the absence of spitz. Missing;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:19718021;Dbxref=PMID:19718021 P04412 UniProtKB Mutagenesis 793 793 . . . Note=In EGFR-ELP-1. C->R P04412 UniProtKB Mutagenesis 936 936 . . . Note=In EGFR-ELP-B1 and EGFR-ELP-B1RB1. A->T P04412 UniProtKB Mutagenesis 1058 1058 . . . Note=In EGFR-ELP-B1RB1. R->Q P04412 UniProtKB Mutagenesis 1095 1095 . . . Note=Weak interaction with EGFRAP%3B when associated with F-1204%3B F-1218%3B F-1246%3B F-1271%3B F-1310%3B F-1342. Very weak interaction with EGFRAP%3B when associated with F-1204%3B F-1218%3B F-1246%3B F-1271%3B F-1310%3B F-1342 and 1405-F-F-1406. Y->F;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:34411095;Dbxref=PMID:34411095 P04412 UniProtKB Mutagenesis 1135 1135 . . . Note=In EGFR-2W74. T->I P04412 UniProtKB Mutagenesis 1156 1156 . . . Note=In EGFR-2C82. G->S P04412 UniProtKB Mutagenesis 1162 1162 . . . Note=In EGFR-1F26. P->L P04412 UniProtKB Mutagenesis 1166 1166 . . . Note=In EGFR-2L65. S->L P04412 UniProtKB Mutagenesis 1204 1204 . . . Note=Weak interaction with EGFRAP%3B when associated with F-1095%3B F-1218%3B F-1246%3B F-1271%3B F-1310%3B F-1342. Very weak interaction with EGFRAP%3B when associated with F-1095%3B F-1218%3B F-1246%3B F-1271%3B F-1310%3B F-1342 and 1405-F-F-1406. Y->F;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:34411095;Dbxref=PMID:34411095 P04412 UniProtKB Mutagenesis 1210 1216 . . . Note=In EGFR-2X51. DKFTRLP->EKVHPAA P04412 UniProtKB Mutagenesis 1218 1218 . . . Note=Weak interaction with EGFRAP%3B when associated with F-1095%3B F-1204%3B F-1246%3B F-1271%3B F-1310%3B F-1342. Very weak interaction with EGFRAP%3B when associated with F-1095%3B F-1204%3B F-1246%3B F-1271%3B F-1310%3B F-1342 and 1405-F-F-1406. Y->F;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:34411095;Dbxref=PMID:34411095 P04412 UniProtKB Mutagenesis 1246 1246 . . . Note=Weak interaction with EGFRAP%3B when associated with F-1095%3B F-1204%3B F-1218%3B F-1271%3B F-1310%3B F-1342. Very weak interaction with EGFRAP%3B when associated with F-1095%3B F-1204%3B F-1218%3B F-1271%3B F-1310%3B F-1342 and 1405-F-F-1406. Y->F;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:34411095;Dbxref=PMID:34411095 P04412 UniProtKB Mutagenesis 1271 1271 . . . Note=Cbl-mediated ubiquitination%2C in response to high levels of Egfr ligand spi%2C is impaired resulting in reduced interaction with Graf and thus decreased GEEC-mediated endocytosis and degradation. Weak interaction with EGFRAP%3B when associated with F-1095%3B F-1204%3B F-1218%3B F-1246%3B F-1310%3B F-1342. Very weak interaction with EGFRAP%3B when associated with F-1095%3B F-1204%3B F-1218%3B F-1246%3B F-1310%3B F-1342 and 1405-F-F-1406. Y->F;Ontology_term=ECO:0000269,ECO:0000269;evidence=ECO:0000269|PubMed:28993397,ECO:0000269|PubMed:34411095;Dbxref=PMID:28993397,PMID:34411095 P04412 UniProtKB Mutagenesis 1310 1310 . . . Note=Weak interaction with EGFRAP%3B when associated with F-1095%3B F-1204%3B F-1218%3B F-1246%3B F-1271%3B F-1342. Very weak interaction with EGFRAP%3B when associated with F-1095%3B F-1204%3B F-1218%3B F-1246%3B F-1271%3B F-1342 and 1405-F-F-1406. Y->F;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:34411095;Dbxref=PMID:34411095 P04412 UniProtKB Mutagenesis 1357 1357 . . . Note=No effect on interaction with EGFRAP. Decreased interaction with EGFRAP%3B when associated with 1405-F-F-1406. Very weak interaction with EGFRAP%3B when associated with F-1095%3B F-1204%3B F-1218%3B F-1246%3B F-1271%3B F-1310. Y->F;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:34411095;Dbxref=PMID:34411095 P04412 UniProtKB Mutagenesis 1405 1406 . . . Note=Decreased interaction with EGFRAP%3B when associated with F-1357. YY->FF;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:34411095;Dbxref=PMID:34411095 P04412 UniProtKB Sequence conflict 137 137 . . . Note=K->E;Ontology_term=ECO:0000305;evidence=ECO:0000305 P04412 UniProtKB Sequence conflict 329 331 . . . Note=AVS->GVC;Ontology_term=ECO:0000305;evidence=ECO:0000305 P04412 UniProtKB Sequence conflict 458 458 . . . Note=R->L;Ontology_term=ECO:0000305;evidence=ECO:0000305 P04412 UniProtKB Sequence conflict 789 789 . . . Note=R->C;Ontology_term=ECO:0000305;evidence=ECO:0000305 P04412 UniProtKB Sequence conflict 959 959 . . . Note=P->A;Ontology_term=ECO:0000305;evidence=ECO:0000305 P04412 UniProtKB Sequence conflict 995 995 . . . Note=E->V;Ontology_term=ECO:0000305;evidence=ECO:0000305 P04412 UniProtKB Sequence conflict 1072 1080 . . . Note=QTPSLVKIT->RLLAGEDH;Ontology_term=ECO:0000305;evidence=ECO:0000305 P04412 UniProtKB Sequence conflict 1097 1098 . . . Note=AA->I;Ontology_term=ECO:0000305;evidence=ECO:0000305 P04412 UniProtKB Sequence conflict 1118 1118 . . . Note=T->R;Ontology_term=ECO:0000305;evidence=ECO:0000305 P04412 UniProtKB Sequence conflict 1242 1242 . . . Note=K->E;Ontology_term=ECO:0000305;evidence=ECO:0000305 P04412 UniProtKB Sequence conflict 1265 1265 . . . Note=M->I;Ontology_term=ECO:0000305;evidence=ECO:0000305 P04412 UniProtKB Sequence conflict 1287 1287 . . . Note=R->T;Ontology_term=ECO:0000305;evidence=ECO:0000305 P04412 UniProtKB Sequence conflict 1325 1325 . . . Note=M->I;Ontology_term=ECO:0000305;evidence=ECO:0000305 P04412 UniProtKB Sequence conflict 1383 1383 . . . Note=G->V;Ontology_term=ECO:0000305;evidence=ECO:0000305 P04412 UniProtKB Sequence conflict 1412 1426 . . . Note=ELQPLHRNRNTETRV->SCSHASKPQHGDEGVGSSRVGAIANEEGESCQVPLEAMRYAFAGCYLR;Ontology_term=ECO:0000305;evidence=ECO:0000305 P04412 UniProtKB Beta strand 101 103 . . . Ontology_term=ECO:0007829;evidence=ECO:0007829|PDB:3I2T P04412 UniProtKB Helix 115 126 . . . Ontology_term=ECO:0007829;evidence=ECO:0007829|PDB:3I2T P04412 UniProtKB Beta strand 131 134 . . . Ontology_term=ECO:0007829;evidence=ECO:0007829|PDB:3I2T P04412 UniProtKB Beta strand 136 141 . . . Ontology_term=ECO:0007829;evidence=ECO:0007829|PDB:3I2T P04412 UniProtKB Helix 149 151 . . . Ontology_term=ECO:0007829;evidence=ECO:0007829|PDB:3I2T P04412 UniProtKB Beta strand 156 159 . . . Ontology_term=ECO:0007829;evidence=ECO:0007829|PDB:3I2T P04412 UniProtKB Beta strand 161 166 . . . Ontology_term=ECO:0007829;evidence=ECO:0007829|PDB:3I2T P04412 UniProtKB Beta strand 169 172 . . . Ontology_term=ECO:0007829;evidence=ECO:0007829|PDB:3I2T P04412 UniProtKB Beta strand 194 200 . . . Ontology_term=ECO:0007829;evidence=ECO:0007829|PDB:3I2T P04412 UniProtKB Beta strand 204 207 . . . Ontology_term=ECO:0007829;evidence=ECO:0007829|PDB:3I2T P04412 UniProtKB Beta strand 216 223 . . . Ontology_term=ECO:0007829;evidence=ECO:0007829|PDB:3I2T P04412 UniProtKB Turn 230 232 . . . Ontology_term=ECO:0007829;evidence=ECO:0007829|PDB:3I2T P04412 UniProtKB Helix 235 237 . . . Ontology_term=ECO:0007829;evidence=ECO:0007829|PDB:3I2T P04412 UniProtKB Beta strand 239 241 . . . Ontology_term=ECO:0007829;evidence=ECO:0007829|PDB:3LTF P04412 UniProtKB Beta strand 246 248 . . . Ontology_term=ECO:0007829;evidence=ECO:0007829|PDB:3I2T P04412 UniProtKB Beta strand 269 273 . . . Ontology_term=ECO:0007829;evidence=ECO:0007829|PDB:3I2T P04412 UniProtKB Helix 274 276 . . . Ontology_term=ECO:0007829;evidence=ECO:0007829|PDB:3I2T P04412 UniProtKB Beta strand 281 285 . . . Ontology_term=ECO:0007829;evidence=ECO:0007829|PDB:3I2T P04412 UniProtKB Beta strand 287 289 . . . Ontology_term=ECO:0007829;evidence=ECO:0007829|PDB:3I2T P04412 UniProtKB Beta strand 290 292 . . . Ontology_term=ECO:0007829;evidence=ECO:0007829|PDB:3LTF P04412 UniProtKB Beta strand 295 300 . . . Ontology_term=ECO:0007829;evidence=ECO:0007829|PDB:3I2T P04412 UniProtKB Beta strand 305 316 . . . Ontology_term=ECO:0007829;evidence=ECO:0007829|PDB:3I2T P04412 UniProtKB Beta strand 319 327 . . . Ontology_term=ECO:0007829;evidence=ECO:0007829|PDB:3I2T P04412 UniProtKB Beta strand 330 334 . . . Ontology_term=ECO:0007829;evidence=ECO:0007829|PDB:3I2T P04412 UniProtKB Beta strand 338 342 . . . Ontology_term=ECO:0007829;evidence=ECO:0007829|PDB:3I2T P04412 UniProtKB Turn 343 346 . . . Ontology_term=ECO:0007829;evidence=ECO:0007829|PDB:3I2T P04412 UniProtKB Beta strand 347 350 . . . Ontology_term=ECO:0007829;evidence=ECO:0007829|PDB:3I2T P04412 UniProtKB Beta strand 356 358 . . . Ontology_term=ECO:0007829;evidence=ECO:0007829|PDB:3I2T P04412 UniProtKB Beta strand 361 365 . . . Ontology_term=ECO:0007829;evidence=ECO:0007829|PDB:3I2T P04412 UniProtKB Beta strand 370 373 . . . Ontology_term=ECO:0007829;evidence=ECO:0007829|PDB:3I2T P04412 UniProtKB Beta strand 376 380 . . . Ontology_term=ECO:0007829;evidence=ECO:0007829|PDB:3I2T P04412 UniProtKB Beta strand 385 394 . . . Ontology_term=ECO:0007829;evidence=ECO:0007829|PDB:3I2T P04412 UniProtKB Beta strand 396 398 . . . Ontology_term=ECO:0007829;evidence=ECO:0007829|PDB:3I2T P04412 UniProtKB Beta strand 402 404 . . . Ontology_term=ECO:0007829;evidence=ECO:0007829|PDB:3I2T P04412 UniProtKB Turn 411 413 . . . Ontology_term=ECO:0007829;evidence=ECO:0007829|PDB:3I2T P04412 UniProtKB Helix 414 417 . . . Ontology_term=ECO:0007829;evidence=ECO:0007829|PDB:3I2T P04412 UniProtKB Beta strand 421 425 . . . Ontology_term=ECO:0007829;evidence=ECO:0007829|PDB:3I2T P04412 UniProtKB Beta strand 427 429 . . . Ontology_term=ECO:0007829;evidence=ECO:0007829|PDB:3I2T P04412 UniProtKB Helix 431 435 . . . Ontology_term=ECO:0007829;evidence=ECO:0007829|PDB:3I2T P04412 UniProtKB Beta strand 438 440 . . . Ontology_term=ECO:0007829;evidence=ECO:0007829|PDB:3I2T P04412 UniProtKB Turn 442 444 . . . Ontology_term=ECO:0007829;evidence=ECO:0007829|PDB:3LTG P04412 UniProtKB Beta strand 446 449 . . . Ontology_term=ECO:0007829;evidence=ECO:0007829|PDB:3I2T P04412 UniProtKB Helix 455 463 . . . Ontology_term=ECO:0007829;evidence=ECO:0007829|PDB:3I2T P04412 UniProtKB Beta strand 466 469 . . . Ontology_term=ECO:0007829;evidence=ECO:0007829|PDB:3I2T P04412 UniProtKB Beta strand 471 473 . . . Ontology_term=ECO:0007829;evidence=ECO:0007829|PDB:3I2T P04412 UniProtKB Helix 484 486 . . . Ontology_term=ECO:0007829;evidence=ECO:0007829|PDB:3I2T P04412 UniProtKB Beta strand 491 493 . . . Ontology_term=ECO:0007829;evidence=ECO:0007829|PDB:3LTF P04412 UniProtKB Turn 499 502 . . . Ontology_term=ECO:0007829;evidence=ECO:0007829|PDB:3I2T P04412 UniProtKB Beta strand 503 509 . . . Ontology_term=ECO:0007829;evidence=ECO:0007829|PDB:3I2T P04412 UniProtKB Beta strand 525 531 . . . Ontology_term=ECO:0007829;evidence=ECO:0007829|PDB:3I2T P04412 UniProtKB Turn 539 541 . . . Ontology_term=ECO:0007829;evidence=ECO:0007829|PDB:3I2T P04412 UniProtKB Helix 544 547 . . . Ontology_term=ECO:0007829;evidence=ECO:0007829|PDB:3I2T P04412 UniProtKB Beta strand 555 561 . . . Ontology_term=ECO:0007829;evidence=ECO:0007829|PDB:3I2T P04412 UniProtKB Helix 563 567 . . . Ontology_term=ECO:0007829;evidence=ECO:0007829|PDB:3I2T P04412 UniProtKB Turn 568 570 . . . Ontology_term=ECO:0007829;evidence=ECO:0007829|PDB:3I2T P04412 UniProtKB Beta strand 575 577 . . . Ontology_term=ECO:0007829;evidence=ECO:0007829|PDB:3LTG P04412 UniProtKB Beta strand 582 586 . . . Ontology_term=ECO:0007829;evidence=ECO:0007829|PDB:3I2T P04412 UniProtKB Beta strand 590 598 . . . Ontology_term=ECO:0007829;evidence=ECO:0007829|PDB:3I2T P04412 UniProtKB Beta strand 601 604 . . . Ontology_term=ECO:0007829;evidence=ECO:0007829|PDB:3I2T P04412 UniProtKB Beta strand 608 610 . . . Ontology_term=ECO:0007829;evidence=ECO:0007829|PDB:3I2T P04412 UniProtKB Beta strand 616 618 . . . Ontology_term=ECO:0007829;evidence=ECO:0007829|PDB:3I2T P04412 UniProtKB Beta strand 628 630 . . . Ontology_term=ECO:0007829;evidence=ECO:0007829|PDB:3I2T P04412 UniProtKB Beta strand 632 636 . . . Ontology_term=ECO:0007829;evidence=ECO:0007829|PDB:3LTF P04412 UniProtKB Beta strand 638 640 . . . Ontology_term=ECO:0007829;evidence=ECO:0007829|PDB:3I2T