##gff-version 3 Q61097 UniProtKB Chain 1 873 . . . ID=PRO_0000086230;Note=Kinase suppressor of Ras 1 Q61097 UniProtKB Domain 563 833 . . . Note=Protein kinase;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00159 Q61097 UniProtKB Zinc finger 333 377 . . . Note=Phorbol-ester/DAG-type;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00226 Q61097 UniProtKB Region 1 170 . . . Note=Mediates association with membranes;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:23250398;Dbxref=PMID:23250398 Q61097 UniProtKB Region 1 24 . . . Note=Disordered;Ontology_term=ECO:0000256;evidence=ECO:0000256|SAM:MobiDB-lite Q61097 UniProtKB Region 174 230 . . . Note=Disordered;Ontology_term=ECO:0000256;evidence=ECO:0000256|SAM:MobiDB-lite Q61097 UniProtKB Region 251 281 . . . Note=Disordered;Ontology_term=ECO:0000256;evidence=ECO:0000256|SAM:MobiDB-lite Q61097 UniProtKB Region 416 473 . . . Note=Disordered;Ontology_term=ECO:0000256;evidence=ECO:0000256|SAM:MobiDB-lite Q61097 UniProtKB Region 506 544 . . . Note=Disordered;Ontology_term=ECO:0000256;evidence=ECO:0000256|SAM:MobiDB-lite Q61097 UniProtKB Compositional bias 202 220 . . . Note=Polar residues;Ontology_term=ECO:0000256;evidence=ECO:0000256|SAM:MobiDB-lite Q61097 UniProtKB Compositional bias 424 473 . . . Note=Polar residues;Ontology_term=ECO:0000256;evidence=ECO:0000256|SAM:MobiDB-lite Q61097 UniProtKB Compositional bias 514 529 . . . Note=Acidic residues;Ontology_term=ECO:0000256;evidence=ECO:0000256|SAM:MobiDB-lite Q61097 UniProtKB Active site 683 683 . . . Note=Proton acceptor;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU10027 Q61097 UniProtKB Binding site 334 334 . . . Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:11786023;Dbxref=PMID:11786023 Q61097 UniProtKB Binding site 346 346 . . . Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:11786023;Dbxref=PMID:11786023 Q61097 UniProtKB Binding site 349 349 . . . Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:11786023;Dbxref=PMID:11786023 Q61097 UniProtKB Binding site 359 359 . . . Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:11786023;Dbxref=PMID:11786023 Q61097 UniProtKB Binding site 362 362 . . . Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:11786023;Dbxref=PMID:11786023 Q61097 UniProtKB Binding site 367 367 . . . Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:11786023;Dbxref=PMID:11786023 Q61097 UniProtKB Binding site 370 370 . . . Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:11786023;Dbxref=PMID:11786023 Q61097 UniProtKB Binding site 377 377 . . . Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:11786023;Dbxref=PMID:11786023 Q61097 UniProtKB Binding site 569 577 . . . Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00159 Q61097 UniProtKB Binding site 685 685 . . . Ontology_term=ECO:0000250;evidence=ECO:0000250|UniProtKB:Q6VAB6 Q61097 UniProtKB Binding site 700 700 . . . Ontology_term=ECO:0000250;evidence=ECO:0000250|UniProtKB:Q6VAB6 Q61097 UniProtKB Modified residue 256 256 . . . Note=Phosphothreonine;Ontology_term=ECO:0000250;evidence=ECO:0000250|UniProtKB:Q8IVT5 Q61097 UniProtKB Modified residue 260 260 . . . Note=Phosphothreonine;Ontology_term=ECO:0000250;evidence=ECO:0000250|UniProtKB:Q8IVT5 Q61097 UniProtKB Modified residue 297 297 . . . Note=Phosphoserine%3B by MARK3;Ontology_term=ECO:0000269,ECO:0000269;evidence=ECO:0000269|PubMed:11741534,ECO:0000269|PubMed:12941695;Dbxref=PMID:11741534,PMID:12941695 Q61097 UniProtKB Modified residue 320 320 . . . Note=Phosphoserine;Ontology_term=ECO:0007744;evidence=ECO:0007744|PubMed:21183079;Dbxref=PMID:21183079 Q61097 UniProtKB Modified residue 337 337 . . . Note=Phosphoserine;Ontology_term=ECO:0000250;evidence=ECO:0000250|UniProtKB:Q8IVT5 Q61097 UniProtKB Modified residue 392 392 . . . Note=Phosphoserine%3B by MARK3;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:12941695;Dbxref=PMID:12941695 Q61097 UniProtKB Modified residue 411 411 . . . Note=Phosphothreonine;Ontology_term=ECO:0000250;evidence=ECO:0000250|UniProtKB:Q8IVT5 Q61097 UniProtKB Modified residue 518 518 . . . Note=Phosphoserine;Ontology_term=ECO:0007744;evidence=ECO:0007744|PubMed:21183079;Dbxref=PMID:21183079 Q61097 UniProtKB Modified residue 838 838 . . . Note=Phosphoserine;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:21102438;Dbxref=PMID:21102438 Q61097 UniProtKB Alternative sequence 474 474 . . . ID=VSP_012232;Note=In isoform 2. P->PAAYFIHHRQQFIFP;Ontology_term=ECO:0000305;evidence=ECO:0000305 Q61097 UniProtKB Alternative sequence 848 873 . . . ID=VSP_012233;Note=In isoform 2. DINSSKVMPRFERFGLGTLESGNPKM->EL;Ontology_term=ECO:0000305;evidence=ECO:0000305 Q61097 UniProtKB Mutagenesis 56 57 . . . Note=No effect on the interaction with MAP2K1%2C MAP2K2 and YWHAE. Abolishes interaction with BRAF. Abolishes location at membrane ruffles. LR->GS;Ontology_term=ECO:0000269,ECO:0000269;evidence=ECO:0000269|PubMed:10409742,ECO:0000269|PubMed:23250398;Dbxref=PMID:10409742,PMID:23250398 Q61097 UniProtKB Mutagenesis 71 71 . . . Note=Impairs interaction with BRAF and association with membrane ruffles%3B when associated with A-78. I->A;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:23250398;Dbxref=PMID:23250398 Q61097 UniProtKB Mutagenesis 78 78 . . . Note=Impairs interaction with BRAF and association with membrane ruffles%3B when associated with A-78. L->A;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:23250398;Dbxref=PMID:23250398 Q61097 UniProtKB Mutagenesis 297 297 . . . Note=Constitutive targeting to the plasma membrane%3B when associated with A-392. S->A;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:11741534;Dbxref=PMID:11741534 Q61097 UniProtKB Mutagenesis 382 382 . . . Note=No effect on interaction with MARK3. L->A;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:12941695;Dbxref=PMID:12941695 Q61097 UniProtKB Mutagenesis 387 387 . . . Note=Reduces interaction with MARK3. Reduces phosphorylation of S-392 by MARK3. L->A;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:12941695;Dbxref=PMID:12941695 Q61097 UniProtKB Mutagenesis 389 389 . . . Note=Reduces phosphorylation of S-392 by MARK3. R->A;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:12941695;Dbxref=PMID:12941695 Q61097 UniProtKB Mutagenesis 390 390 . . . Note=No effect on phosphorylation of S-392 by MARK3. T->A;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:12941695;Dbxref=PMID:12941695 Q61097 UniProtKB Mutagenesis 391 391 . . . Note=No effect on phosphorylation of S-392 by MARK3. E->A;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:12941695;Dbxref=PMID:12941695 Q61097 UniProtKB Mutagenesis 392 392 . . . Note=Constitutive targeting to the plasma membrane%3B when associated with A-297. No effect on interaction with MARK3. Abolishes phosphorylation by MARK3. S->A;Ontology_term=ECO:0000269,ECO:0000269;evidence=ECO:0000269|PubMed:11741534,ECO:0000269|PubMed:12941695;Dbxref=PMID:11741534,PMID:12941695 Q61097 UniProtKB Mutagenesis 393 393 . . . Note=Reduces phosphorylation of S-392 by MARK3. V->A;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:12941695;Dbxref=PMID:12941695 Q61097 UniProtKB Mutagenesis 394 394 . . . Note=No effect on phosphorylation of S-392 by MARK3. P->A;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:12941695;Dbxref=PMID:12941695 Q61097 UniProtKB Mutagenesis 395 395 . . . Note=No effect on phosphorylation of S-392 by MARK3. S->A;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:12941695;Dbxref=PMID:12941695 Q61097 UniProtKB Mutagenesis 396 396 . . . Note=No effect on phosphorylation of S-392 by MARK3. D->A;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:12941695;Dbxref=PMID:12941695 Q61097 UniProtKB Mutagenesis 397 397 . . . Note=Decrease in MARK3 binding%3B when associated with A-401. Abolishes interaction with MARK3. Reduces phosphorylation of S-392 by MARK3. I->A;Ontology_term=ECO:0000269,ECO:0000269;evidence=ECO:0000269|PubMed:11741534,ECO:0000269|PubMed:12941695;Dbxref=PMID:11741534,PMID:12941695 Q61097 UniProtKB Mutagenesis 400 400 . . . Note=No effect on interaction with MARK3. P->A;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:12941695;Dbxref=PMID:12941695 Q61097 UniProtKB Mutagenesis 401 401 . . . Note=Decrease in MARK3 binding%3B when associated with A-397. No effect on interaction with MARK3. V->A;Ontology_term=ECO:0000269,ECO:0000269;evidence=ECO:0000269|PubMed:11741534,ECO:0000269|PubMed:12941695;Dbxref=PMID:11741534,PMID:12941695 Q61097 UniProtKB Mutagenesis 403 403 . . . Note=No effect on interaction with MARK3. R->A;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:12941695;Dbxref=PMID:12941695 Q61097 UniProtKB Mutagenesis 413 413 . . . Note=No effect on interaction with MARK3. P->A;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:12941695;Dbxref=PMID:12941695 Q61097 UniProtKB Mutagenesis 572 572 . . . Note=Decrease in MEK binding. G->E;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:10891492;Dbxref=PMID:10891492 Q61097 UniProtKB Mutagenesis 580 580 . . . Note=Partial decrease in MAP2K1 and MAP2K2 binding. No effect on the interaction with YWHAE. G->E;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:10409742;Dbxref=PMID:10409742 Q61097 UniProtKB Mutagenesis 587 587 . . . Note=Loss of ATP binding and reduces MAPK1 and MAPK3 phosphorylation levels. Loss of kinase activity towards MAP2K1 in vitro. Abnormal constitutive interaction with CRAF. No effect on the interaction with BRAF and MAP2K1. A->F;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:21441104;Dbxref=PMID:21441104 Q61097 UniProtKB Mutagenesis 587 587 . . . Note=No effect on ATP binding and MAPK1 and MAPK3 phosphorylation levels. No effect on the interaction with MAP2K1. A->V;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:21441104;Dbxref=PMID:21441104 Q61097 UniProtKB Mutagenesis 589 589 . . . Note=Severe decrease in MAP2K1 and MAP2K2 binding. No effect on the interaction with YWHAE. R->M;Ontology_term=ECO:0000269,ECO:0000269;evidence=ECO:0000269|PubMed:10409742,ECO:0000269|PubMed:10891492;Dbxref=PMID:10409742,PMID:10891492 Q61097 UniProtKB Mutagenesis 615 615 . . . Note=Severe decrease in MAP2K1 and MAP2K2 binding. No effect on the interaction with YWHAE. R->H;Ontology_term=ECO:0000269,ECO:0000269;evidence=ECO:0000269|PubMed:10409742,ECO:0000269|PubMed:10891492;Dbxref=PMID:10409742,PMID:10891492 Q61097 UniProtKB Mutagenesis 700 700 . . . Note=Decrease in MEK binding. D->V;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:10891492;Dbxref=PMID:10891492 Q61097 UniProtKB Mutagenesis 809 809 . . . Note=Associates almost exclusively with the membrane. Loss of MAP2K2 and MAP2K2 binding and recruitment to the membrane. Loss of MAP kinase-mediated inhibition of ELK1 phosphorylation. No effect on the interaction with YWHAE. C->Y;Ontology_term=ECO:0000269,ECO:0000269;evidence=ECO:0000269|PubMed:10409742,ECO:0000269|PubMed:10891492;Dbxref=PMID:10409742,PMID:10891492 Q61097 UniProtKB Mutagenesis 838 838 . . . Note=Abolishes one phosphorylation site. Decreases phosphorylation by PKA. S->A;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:21102438;Dbxref=PMID:21102438 Q61097 UniProtKB Turn 30 32 . . . Ontology_term=ECO:0007829;evidence=ECO:0007829|PDB:2LPE Q61097 UniProtKB Helix 33 36 . . . Ontology_term=ECO:0007829;evidence=ECO:0007829|PDB:2LPE Q61097 UniProtKB Helix 37 39 . . . Ontology_term=ECO:0007829;evidence=ECO:0007829|PDB:2LPE Q61097 UniProtKB Helix 47 58 . . . Ontology_term=ECO:0007829;evidence=ECO:0007829|PDB:2LPE Q61097 UniProtKB Helix 65 82 . . . Ontology_term=ECO:0007829;evidence=ECO:0007829|PDB:2LPE Q61097 UniProtKB Helix 83 85 . . . Ontology_term=ECO:0007829;evidence=ECO:0007829|PDB:2LPE Q61097 UniProtKB Helix 88 90 . . . Ontology_term=ECO:0007829;evidence=ECO:0007829|PDB:2LPE Q61097 UniProtKB Turn 94 96 . . . Ontology_term=ECO:0007829;evidence=ECO:0007829|PDB:2LPE Q61097 UniProtKB Helix 101 103 . . . Ontology_term=ECO:0007829;evidence=ECO:0007829|PDB:2LPE Q61097 UniProtKB Turn 108 110 . . . Ontology_term=ECO:0007829;evidence=ECO:0007829|PDB:2LPE Q61097 UniProtKB Helix 111 114 . . . Ontology_term=ECO:0007829;evidence=ECO:0007829|PDB:2LPE Q61097 UniProtKB Helix 118 121 . . . Ontology_term=ECO:0007829;evidence=ECO:0007829|PDB:2LPE Q61097 UniProtKB Helix 130 133 . . . Ontology_term=ECO:0007829;evidence=ECO:0007829|PDB:2LPE Q61097 UniProtKB Helix 138 146 . . . Ontology_term=ECO:0007829;evidence=ECO:0007829|PDB:2LPE Q61097 UniProtKB Turn 147 149 . . . Ontology_term=ECO:0007829;evidence=ECO:0007829|PDB:2LPE Q61097 UniProtKB Helix 153 162 . . . Ontology_term=ECO:0007829;evidence=ECO:0007829|PDB:2LPE Q61097 UniProtKB Helix 163 167 . . . Ontology_term=ECO:0007829;evidence=ECO:0007829|PDB:2LPE Q61097 UniProtKB Beta strand 336 339 . . . Ontology_term=ECO:0007829;evidence=ECO:0007829|PDB:1KBE Q61097 UniProtKB Beta strand 347 349 . . . Ontology_term=ECO:0007829;evidence=ECO:0007829|PDB:1KBE Q61097 UniProtKB Beta strand 356 359 . . . Ontology_term=ECO:0007829;evidence=ECO:0007829|PDB:1KBE Q61097 UniProtKB Turn 360 363 . . . Ontology_term=ECO:0007829;evidence=ECO:0007829|PDB:1KBE Q61097 UniProtKB Beta strand 364 369 . . . Ontology_term=ECO:0007829;evidence=ECO:0007829|PDB:1KBE Q61097 UniProtKB Turn 371 373 . . . Ontology_term=ECO:0007829;evidence=ECO:0007829|PDB:1KBE