##gff-version 3 Q05512 UniProtKB Chain 1 776 . . . ID=PRO_0000086302;Note=Serine/threonine-protein kinase MARK2 Q05512 UniProtKB Domain 53 304 . . . Note=Protein kinase;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00159 Q05512 UniProtKB Domain 323 362 . . . Note=UBA;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00212 Q05512 UniProtKB Domain 727 776 . . . Note=KA1;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00565 Q05512 UniProtKB Region 1 46 . . . Note=Disordered;Ontology_term=ECO:0000256;evidence=ECO:0000256|SAM:MobiDB-lite Q05512 UniProtKB Region 373 630 . . . Note=Disordered;Ontology_term=ECO:0000256;evidence=ECO:0000256|SAM:MobiDB-lite Q05512 UniProtKB Compositional bias 378 429 . . . Note=Polar residues;Ontology_term=ECO:0000256;evidence=ECO:0000256|SAM:MobiDB-lite Q05512 UniProtKB Compositional bias 430 444 . . . Note=Basic and acidic residues;Ontology_term=ECO:0000256;evidence=ECO:0000256|SAM:MobiDB-lite Q05512 UniProtKB Compositional bias 463 630 . . . Note=Polar residues;Ontology_term=ECO:0000256;evidence=ECO:0000256|SAM:MobiDB-lite Q05512 UniProtKB Active site 175 175 . . . Note=Proton acceptor;Ontology_term=ECO:0000255,ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00159,ECO:0000255|PROSITE-ProRule:PRU10027 Q05512 UniProtKB Binding site 59 67 . . . Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00159 Q05512 UniProtKB Binding site 82 82 . . . Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00159 Q05512 UniProtKB Modified residue 40 40 . . . Note=Phosphoserine;Ontology_term=ECO:0000250;evidence=ECO:0000250|UniProtKB:Q7KZI7 Q05512 UniProtKB Modified residue 58 58 . . . Note=Phosphothreonine%3B by autocatalysis;Ontology_term=ECO:0000250;evidence=ECO:0000250|UniProtKB:O08679 Q05512 UniProtKB Modified residue 91 91 . . . Note=Phosphoserine%3B by CaMK1;Ontology_term=ECO:0000250;evidence=ECO:0000250|UniProtKB:O08679 Q05512 UniProtKB Modified residue 92 92 . . . Note=Phosphoserine%3B by CaMK1;Ontology_term=ECO:0000250;evidence=ECO:0000250|UniProtKB:O08679 Q05512 UniProtKB Modified residue 93 93 . . . Note=Phosphoserine%3B by CaMK1;Ontology_term=ECO:0000250;evidence=ECO:0000250|UniProtKB:O08679 Q05512 UniProtKB Modified residue 208 208 . . . Note=Phosphothreonine%3B by LKB1 and TAOK1;Ontology_term=ECO:0000250;evidence=ECO:0000250|UniProtKB:Q7KZI7 Q05512 UniProtKB Modified residue 212 212 . . . Note=Phosphoserine%3B by GSK3-beta;Ontology_term=ECO:0000250;evidence=ECO:0000250|UniProtKB:O08679 Q05512 UniProtKB Modified residue 274 274 . . . Note=Phosphoserine%3B by autocatalysis;Ontology_term=ECO:0000250;evidence=ECO:0000250|UniProtKB:O08679 Q05512 UniProtKB Modified residue 275 275 . . . Note=Phosphothreonine%3B by autocatalysis;Ontology_term=ECO:0000250;evidence=ECO:0000250|UniProtKB:O08679 Q05512 UniProtKB Modified residue 294 294 . . . Note=Phosphothreonine%3B by CaMK1;Ontology_term=ECO:0000250;evidence=ECO:0000250|UniProtKB:O08679 Q05512 UniProtKB Modified residue 408 408 . . . Note=Phosphoserine;Ontology_term=ECO:0000250;evidence=ECO:0000250|UniProtKB:O08679 Q05512 UniProtKB Modified residue 409 409 . . . Note=Phosphoserine;Ontology_term=ECO:0000250;evidence=ECO:0000250|UniProtKB:Q7KZI7 Q05512 UniProtKB Modified residue 453 453 . . . Note=Phosphoserine;Ontology_term=ECO:0007744,ECO:0007744;evidence=ECO:0007744|PubMed:19144319,ECO:0007744|PubMed:21183079;Dbxref=PMID:19144319,PMID:21183079 Q05512 UniProtKB Modified residue 464 464 . . . Note=Phosphothreonine;Ontology_term=ECO:0000250;evidence=ECO:0000250|UniProtKB:Q7KZI7 Q05512 UniProtKB Modified residue 483 483 . . . Note=Phosphoserine;Ontology_term=ECO:0007744;evidence=ECO:0007744|PubMed:21183079;Dbxref=PMID:21183079 Q05512 UniProtKB Modified residue 490 490 . . . Note=Phosphoserine;Ontology_term=ECO:0000250;evidence=ECO:0000250|UniProtKB:Q7KZI7 Q05512 UniProtKB Modified residue 566 566 . . . Note=Phosphoserine;Ontology_term=ECO:0000250;evidence=ECO:0000250|UniProtKB:Q7KZI7 Q05512 UniProtKB Modified residue 568 568 . . . Note=Phosphoserine;Ontology_term=ECO:0007744;evidence=ECO:0007744|PubMed:21183079;Dbxref=PMID:21183079 Q05512 UniProtKB Modified residue 589 589 . . . Note=Phosphoserine;Ontology_term=ECO:0000250;evidence=ECO:0000250|UniProtKB:Q7KZI7 Q05512 UniProtKB Modified residue 593 593 . . . Note=Phosphothreonine%3B by PKC/PRKCZ;Ontology_term=ECO:0000250;evidence=ECO:0000250|UniProtKB:Q7KZI7 Q05512 UniProtKB Modified residue 616 616 . . . Note=Phosphoserine;Ontology_term=ECO:0000250;evidence=ECO:0000250|UniProtKB:Q7KZI7 Q05512 UniProtKB Modified residue 710 710 . . . Note=Phosphoserine;Ontology_term=ECO:0000250;evidence=ECO:0000250|UniProtKB:Q7KZI7 Q05512 UniProtKB Alternative sequence 321 339 . . . ID=VSP_013341;Note=In isoform 2. PDYKDPRRTELMVSMGYTR->LTTGPRDRVDGVNGLHT;Ontology_term=ECO:0000303;evidence=ECO:0000303|PubMed:8358177;Dbxref=PMID:8358177 Q05512 UniProtKB Alternative sequence 502 555 . . . ID=VSP_013342;Note=In isoform 3 and isoform 4. Missing;Ontology_term=ECO:0000303,ECO:0000303;evidence=ECO:0000303|PubMed:15489334,ECO:0000303|PubMed:16141072;Dbxref=PMID:15489334,PMID:16141072 Q05512 UniProtKB Alternative sequence 640 640 . . . ID=VSP_022597;Note=In isoform 4. V->VRRNLSFRFA;Ontology_term=ECO:0000303;evidence=ECO:0000303|PubMed:16141072;Dbxref=PMID:16141072 Q05512 UniProtKB Sequence conflict 161 162 . . . Note=SA->LH;Ontology_term=ECO:0000305;evidence=ECO:0000305 Q05512 UniProtKB Sequence conflict 368 368 . . . Note=L->P;Ontology_term=ECO:0000305;evidence=ECO:0000305 Q05512 UniProtKB Sequence conflict 760 760 . . . Note=S->Y;Ontology_term=ECO:0000305;evidence=ECO:0000305