##gff-version 3 O08678 UniProtKB Chain 1 793 . . . ID=PRO_0000086300;Note=Serine/threonine-protein kinase MARK1 O08678 UniProtKB Domain 60 311 . . . Note=Protein kinase;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00159 O08678 UniProtKB Domain 329 370 . . . Note=UBA;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00212 O08678 UniProtKB Domain 744 793 . . . Note=KA1;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00565 O08678 UniProtKB Region 1 40 . . . Note=Disordered;Ontology_term=ECO:0000256;evidence=ECO:0000256|SAM:MobiDB-lite O08678 UniProtKB Region 377 499 . . . Note=Disordered;Ontology_term=ECO:0000256;evidence=ECO:0000256|SAM:MobiDB-lite O08678 UniProtKB Region 517 697 . . . Note=Disordered;Ontology_term=ECO:0000256;evidence=ECO:0000256|SAM:MobiDB-lite O08678 UniProtKB Compositional bias 22 40 . . . Note=Polar residues;Ontology_term=ECO:0000256;evidence=ECO:0000256|SAM:MobiDB-lite O08678 UniProtKB Compositional bias 381 423 . . . Note=Polar residues;Ontology_term=ECO:0000256;evidence=ECO:0000256|SAM:MobiDB-lite O08678 UniProtKB Compositional bias 444 459 . . . Note=Basic and acidic residues;Ontology_term=ECO:0000256;evidence=ECO:0000256|SAM:MobiDB-lite O08678 UniProtKB Compositional bias 485 499 . . . Note=Polar residues;Ontology_term=ECO:0000256;evidence=ECO:0000256|SAM:MobiDB-lite O08678 UniProtKB Compositional bias 517 563 . . . Note=Polar residues;Ontology_term=ECO:0000256;evidence=ECO:0000256|SAM:MobiDB-lite O08678 UniProtKB Compositional bias 586 614 . . . Note=Polar residues;Ontology_term=ECO:0000256;evidence=ECO:0000256|SAM:MobiDB-lite O08678 UniProtKB Compositional bias 679 697 . . . Note=Basic and acidic residues;Ontology_term=ECO:0000256;evidence=ECO:0000256|SAM:MobiDB-lite O08678 UniProtKB Active site 182 182 . . . Note=Proton acceptor;Ontology_term=ECO:0000250,ECO:0000255,ECO:0000255;evidence=ECO:0000250|UniProtKB:Q9H0K1,ECO:0000255|PROSITE-ProRule:PRU00159,ECO:0000255|PROSITE-ProRule:PRU10027 O08678 UniProtKB Binding site 66 74 . . . Ontology_term=ECO:0000250,ECO:0000255;evidence=ECO:0000250|UniProtKB:Q9H0K1,ECO:0000255|PROSITE-ProRule:PRU00159 O08678 UniProtKB Binding site 89 89 . . . Ontology_term=ECO:0000255,ECO:0000269;evidence=ECO:0000255|PROSITE-ProRule:PRU00159,ECO:0000269|PubMed:9108484;Dbxref=PMID:9108484 O08678 UniProtKB Modified residue 5 5 . . . Note=Phosphothreonine;Ontology_term=ECO:0000250;evidence=ECO:0000250|UniProtKB:Q9P0L2 O08678 UniProtKB Modified residue 208 208 . . . Note=Phosphothreonine;Ontology_term=ECO:0000250;evidence=ECO:0000250|UniProtKB:Q9P0L2 O08678 UniProtKB Modified residue 215 215 . . . Note=Phosphothreonine%3B by LKB1 and TAOK1;Ontology_term=ECO:0000269,ECO:0000269;evidence=ECO:0000269|PubMed:14517247,ECO:0000269|PubMed:9108484;Dbxref=PMID:14517247,PMID:9108484 O08678 UniProtKB Modified residue 219 219 . . . Note=Phosphoserine%3B by GSK3-beta;Ontology_term=ECO:0000269,ECO:0000269;evidence=ECO:0000269|PubMed:14517247,ECO:0000269|PubMed:9108484;Dbxref=PMID:14517247,PMID:9108484 O08678 UniProtKB Modified residue 382 382 . . . Note=Phosphoserine;Ontology_term=ECO:0000250;evidence=ECO:0000250|UniProtKB:Q8VHJ5 O08678 UniProtKB Modified residue 390 390 . . . Note=Phosphoserine;Ontology_term=ECO:0000250;evidence=ECO:0000250|UniProtKB:Q8VHJ5 O08678 UniProtKB Modified residue 393 393 . . . Note=Phosphoserine;Ontology_term=ECO:0000250;evidence=ECO:0000250|UniProtKB:Q8VHJ5 O08678 UniProtKB Modified residue 403 403 . . . Note=Phosphoserine;Ontology_term=ECO:0000250;evidence=ECO:0000250|UniProtKB:Q9P0L2 O08678 UniProtKB Modified residue 423 423 . . . Note=Phosphoserine;Ontology_term=ECO:0000250;evidence=ECO:0000250|UniProtKB:Q8VHJ5 O08678 UniProtKB Modified residue 444 444 . . . Note=Phosphoserine;Ontology_term=ECO:0007744;evidence=ECO:0007744|PubMed:22673903;Dbxref=PMID:22673903 O08678 UniProtKB Modified residue 475 475 . . . Note=Phosphoserine;Ontology_term=ECO:0000250;evidence=ECO:0000250|UniProtKB:Q8VHJ5 O08678 UniProtKB Modified residue 588 588 . . . Note=Phosphoserine;Ontology_term=ECO:0000250;evidence=ECO:0000250|UniProtKB:Q9P0L2 O08678 UniProtKB Modified residue 613 613 . . . Note=Phosphothreonine%3B by PKC/PRKCZ;Ontology_term=ECO:0000250;evidence=ECO:0000250 O08678 UniProtKB Modified residue 666 666 . . . Note=Phosphoserine;Ontology_term=ECO:0000250;evidence=ECO:0000250|UniProtKB:Q8VHJ5 O08678 UniProtKB Mutagenesis 89 89 . . . Note=Loss of kinase activity. K->R;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:9108484;Dbxref=PMID:9108484 O08678 UniProtKB Mutagenesis 215 215 . . . Note=Abolishes activation of serine/threonine-protein kinase activity and only basal activity remains. T->A;Ontology_term=ECO:0000269,ECO:0000269;evidence=ECO:0000269|PubMed:14517247,ECO:0000269|PubMed:9108484;Dbxref=PMID:14517247,PMID:9108484 O08678 UniProtKB Mutagenesis 215 215 . . . Note=Loss of kinase activity. T->A;Ontology_term=ECO:0000269,ECO:0000269;evidence=ECO:0000269|PubMed:14517247,ECO:0000269|PubMed:9108484;Dbxref=PMID:14517247,PMID:9108484 O08678 UniProtKB Mutagenesis 215 215 . . . Note=Induces an increase of the basal serine/threonine-protein kinase activity. T->E;Ontology_term=ECO:0000269,ECO:0000269;evidence=ECO:0000269|PubMed:14517247,ECO:0000269|PubMed:9108484;Dbxref=PMID:14517247,PMID:9108484 O08678 UniProtKB Mutagenesis 219 219 . . . Note=Loss of activity. S->A%2CE;Ontology_term=ECO:0000269,ECO:0000269;evidence=ECO:0000269|PubMed:14517247,ECO:0000269|PubMed:9108484;Dbxref=PMID:14517247,PMID:9108484 O08678 UniProtKB Mutagenesis 219 219 . . . Note=Loss of kinase activity. S->A;Ontology_term=ECO:0000269,ECO:0000269;evidence=ECO:0000269|PubMed:14517247,ECO:0000269|PubMed:9108484;Dbxref=PMID:14517247,PMID:9108484