##gff-version 3 Q8NB16 UniProtKB Chain 1 471 . . . ID=PRO_0000248239;Note=Mixed lineage kinase domain-like protein Q8NB16 UniProtKB Domain 194 469 . . . Note=Protein kinase;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00159 Q8NB16 UniProtKB Region 1 149 . . . Note=N-terminal bundle and brace (NBB)%3B mediates INSP6 binding;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:29883610;Dbxref=PMID:29883610 Q8NB16 UniProtKB Coiled coil 55 84 . . . Ontology_term=ECO:0000255;evidence=ECO:0000255 Q8NB16 UniProtKB Coiled coil 139 180 . . . Ontology_term=ECO:0000255;evidence=ECO:0000255 Q8NB16 UniProtKB Binding site 209 217 . . . Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00159 Q8NB16 UniProtKB Binding site 230 230 . . . Ontology_term=ECO:0000305;evidence=ECO:0000305 Q8NB16 UniProtKB Site 86 86 . . . Note=Target of necrosulfonamide inhibitor;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:22265413;Dbxref=PMID:22265413 Q8NB16 UniProtKB Modified residue 125 125 . . . Note=Phosphoserine;Ontology_term=ECO:0007744,ECO:0007744;evidence=ECO:0007744|PubMed:18669648,ECO:0007744|PubMed:18691976;Dbxref=PMID:18669648,PMID:18691976 Q8NB16 UniProtKB Modified residue 357 357 . . . Note=Phosphothreonine%3B by RIPK3;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:22265413;Dbxref=PMID:22265413 Q8NB16 UniProtKB Modified residue 358 358 . . . Note=Phosphoserine%3B by RIPK3;Ontology_term=ECO:0000269,ECO:0000269;evidence=ECO:0000269|PubMed:22265413,ECO:0000269|PubMed:29883610;Dbxref=PMID:22265413,PMID:29883610 Q8NB16 UniProtKB Modified residue 360 360 . . . Note=Phosphoserine%3B by RIPK3;Ontology_term=ECO:0000250;evidence=ECO:0000250|UniProtKB:Q9D2Y4 Q8NB16 UniProtKB Alternative sequence 179 205 . . . ID=VSP_052133;Note=In isoform 2. YLPPKCMQEIPQEQIKEIKKEQLSGSP->SLESSSGKSPLEISRFKVKNVKTGSAS;Ontology_term=ECO:0000303;evidence=ECO:0000303|PubMed:15489334;Dbxref=PMID:15489334 Q8NB16 UniProtKB Alternative sequence 206 413 . . . ID=VSP_052134;Note=In isoform 2. Missing;Ontology_term=ECO:0000303;evidence=ECO:0000303|PubMed:15489334;Dbxref=PMID:15489334 Q8NB16 UniProtKB Natural variant 52 52 . . . ID=VAR_041350;Note=S->T;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:17344846;Dbxref=dbSNP:rs34251827,PMID:17344846 Q8NB16 UniProtKB Natural variant 100 100 . . . ID=VAR_041351;Note=D->E;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:17344846;Dbxref=dbSNP:rs33987771,PMID:17344846 Q8NB16 UniProtKB Natural variant 132 132 . . . ID=VAR_041352;Note=S->P;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:17344846;Dbxref=dbSNP:rs35589326,PMID:17344846 Q8NB16 UniProtKB Natural variant 146 146 . . . ID=VAR_041353;Note=R->Q;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:17344846;Dbxref=dbSNP:rs34515646,PMID:17344846 Q8NB16 UniProtKB Natural variant 169 169 . . . ID=VAR_041354;Note=M->L;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:17344846;Dbxref=dbSNP:rs55929310,PMID:17344846 Q8NB16 UniProtKB Natural variant 291 291 . . . ID=VAR_041355;Note=In a gastric adenocarcinoma sample%3B somatic mutation. L->P;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:17344846;Dbxref=dbSNP:rs1313508921,PMID:17344846 Q8NB16 UniProtKB Natural variant 364 364 . . . ID=VAR_041356;Note=T->M;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:17344846;Dbxref=dbSNP:rs34389205,PMID:17344846 Q8NB16 UniProtKB Natural variant 398 398 . . . ID=VAR_041357;Note=In a gastric adenocarcinoma sample%3B somatic mutation. F->I;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:17344846;Dbxref=PMID:17344846 Q8NB16 UniProtKB Natural variant 421 421 . . . ID=VAR_041358;Note=R->H;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:17344846;Dbxref=dbSNP:rs55987292,PMID:17344846 Q8NB16 UniProtKB Mutagenesis 58 58 . . . Note=Does not affect formation of homotrimers%2C while translocation to the plasma membrane on necroptosis induction is impaired%3B when associated with G-76. L->G;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:24316671;Dbxref=PMID:24316671 Q8NB16 UniProtKB Mutagenesis 76 76 . . . Note=Does not affect formation of homotrimers%2C while translocation to the plasma membrane on necroptosis induction is impaired%3B when associated with G-58. I->G;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:24316671;Dbxref=PMID:24316671 Q8NB16 UniProtKB Mutagenesis 86 86 . . . Note=Abolishes binding to necrosulfonamide inhibitor. C->S;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:22265413;Dbxref=PMID:22265413 Q8NB16 UniProtKB Mutagenesis 162 162 . . . Note=Impairs formation of homotrimers and translocation to the plasma membrane on necroptosis induction%3B when associated with G-165. L->G;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:24316671;Dbxref=PMID:24316671 Q8NB16 UniProtKB Mutagenesis 165 165 . . . Note=Impairs formation of homotrimers and translocation to the plasma membrane on necroptosis induction%3B when associated with G-162. L->G;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:24316671;Dbxref=PMID:24316671 Q8NB16 UniProtKB Mutagenesis 230 230 . . . Note=Abolishes ATP-binding. K->M;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:24219132;Dbxref=PMID:24219132 Q8NB16 UniProtKB Mutagenesis 331 331 . . . Note=Impairs ATP-binding. K->N;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:24219132;Dbxref=PMID:24219132 Q8NB16 UniProtKB Mutagenesis 351 351 . . . Note=Binds ATP with an enhanced affinity. E->K;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:24219132;Dbxref=PMID:24219132 Q8NB16 UniProtKB Mutagenesis 357 358 . . . Note=Mimics phosphorylation state%3B acts as a dominant-negative mutant that impairs necroptosis. TS->ED Q8NB16 UniProtKB Mutagenesis 357 357 . . . Note=No effect. Abolishes ability to mediate necroptosis%3B when associated with A-358. T->A;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:22265413;Dbxref=PMID:22265413 Q8NB16 UniProtKB Mutagenesis 358 358 . . . Note=No effect. Abolishes ability to mediate necroptosis%3B when associated with A-357. S->A;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:22265413;Dbxref=PMID:22265413 Q8NB16 UniProtKB Helix 2 20 . . . Ontology_term=ECO:0007829;evidence=ECO:0007829|PDB:6ZVO Q8NB16 UniProtKB Beta strand 22 24 . . . Ontology_term=ECO:0007829;evidence=ECO:0007829|PDB:6ZZ1 Q8NB16 UniProtKB Helix 25 46 . . . Ontology_term=ECO:0007829;evidence=ECO:0007829|PDB:6ZVO Q8NB16 UniProtKB Helix 56 79 . . . Ontology_term=ECO:0007829;evidence=ECO:0007829|PDB:6ZVO Q8NB16 UniProtKB Helix 82 90 . . . Ontology_term=ECO:0007829;evidence=ECO:0007829|PDB:6ZVO Q8NB16 UniProtKB Beta strand 93 96 . . . Ontology_term=ECO:0007829;evidence=ECO:0007829|PDB:2MSV Q8NB16 UniProtKB Helix 99 120 . . . Ontology_term=ECO:0007829;evidence=ECO:0007829|PDB:6ZVO Q8NB16 UniProtKB Turn 128 132 . . . Ontology_term=ECO:0007829;evidence=ECO:0007829|PDB:2MSV Q8NB16 UniProtKB Helix 133 148 . . . Ontology_term=ECO:0007829;evidence=ECO:0007829|PDB:6ZVO Q8NB16 UniProtKB Helix 198 201 . . . Ontology_term=ECO:0007829;evidence=ECO:0007829|PDB:4MWI Q8NB16 UniProtKB Beta strand 202 204 . . . Ontology_term=ECO:0007829;evidence=ECO:0007829|PDB:6O5Z Q8NB16 UniProtKB Beta strand 207 211 . . . Ontology_term=ECO:0007829;evidence=ECO:0007829|PDB:4MWI Q8NB16 UniProtKB Beta strand 213 222 . . . Ontology_term=ECO:0007829;evidence=ECO:0007829|PDB:4MWI Q8NB16 UniProtKB Beta strand 225 232 . . . Ontology_term=ECO:0007829;evidence=ECO:0007829|PDB:4MWI Q8NB16 UniProtKB Helix 240 256 . . . Ontology_term=ECO:0007829;evidence=ECO:0007829|PDB:4MWI Q8NB16 UniProtKB Beta strand 265 271 . . . Ontology_term=ECO:0007829;evidence=ECO:0007829|PDB:4MWI Q8NB16 UniProtKB Beta strand 274 276 . . . Ontology_term=ECO:0007829;evidence=ECO:0007829|PDB:4MWI Q8NB16 UniProtKB Beta strand 278 284 . . . Ontology_term=ECO:0007829;evidence=ECO:0007829|PDB:4MWI Q8NB16 UniProtKB Helix 291 297 . . . Ontology_term=ECO:0007829;evidence=ECO:0007829|PDB:4MWI Q8NB16 UniProtKB Helix 303 322 . . . Ontology_term=ECO:0007829;evidence=ECO:0007829|PDB:4MWI Q8NB16 UniProtKB Beta strand 323 325 . . . Ontology_term=ECO:0007829;evidence=ECO:0007829|PDB:4MWI Q8NB16 UniProtKB Helix 334 336 . . . Ontology_term=ECO:0007829;evidence=ECO:0007829|PDB:4MWI Q8NB16 UniProtKB Beta strand 337 339 . . . Ontology_term=ECO:0007829;evidence=ECO:0007829|PDB:4MWI Q8NB16 UniProtKB Beta strand 345 347 . . . Ontology_term=ECO:0007829;evidence=ECO:0007829|PDB:4MWI Q8NB16 UniProtKB Beta strand 349 352 . . . Ontology_term=ECO:0007829;evidence=ECO:0007829|PDB:7MON Q8NB16 UniProtKB Helix 353 359 . . . Ontology_term=ECO:0007829;evidence=ECO:0007829|PDB:7MON Q8NB16 UniProtKB Turn 360 362 . . . Ontology_term=ECO:0007829;evidence=ECO:0007829|PDB:7JXU Q8NB16 UniProtKB Helix 373 376 . . . Ontology_term=ECO:0007829;evidence=ECO:0007829|PDB:4MWI Q8NB16 UniProtKB Helix 379 383 . . . Ontology_term=ECO:0007829;evidence=ECO:0007829|PDB:4MWI Q8NB16 UniProtKB Helix 391 407 . . . Ontology_term=ECO:0007829;evidence=ECO:0007829|PDB:4MWI Q8NB16 UniProtKB Turn 411 414 . . . Ontology_term=ECO:0007829;evidence=ECO:0007829|PDB:4MWI Q8NB16 UniProtKB Helix 417 425 . . . Ontology_term=ECO:0007829;evidence=ECO:0007829|PDB:4MWI Q8NB16 UniProtKB Beta strand 435 437 . . . Ontology_term=ECO:0007829;evidence=ECO:0007829|PDB:6O5Z Q8NB16 UniProtKB Helix 439 448 . . . Ontology_term=ECO:0007829;evidence=ECO:0007829|PDB:4MWI Q8NB16 UniProtKB Helix 453 455 . . . Ontology_term=ECO:0007829;evidence=ECO:0007829|PDB:4MWI Q8NB16 UniProtKB Helix 459 467 . . . Ontology_term=ECO:0007829;evidence=ECO:0007829|PDB:4MWI