##gff-version 3 Q02078 UniProtKB Chain 1 507 . . . ID=PRO_0000199428;Note=Myocyte-specific enhancer factor 2A Q02078 UniProtKB Domain 3 57 . . . Note=MADS-box;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00251 Q02078 UniProtKB DNA binding 58 86 . . . Note=Mef2-type;Ontology_term=ECO:0000255;evidence=ECO:0000255 Q02078 UniProtKB Region 173 229 . . . Note=Disordered;Ontology_term=ECO:0000256;evidence=ECO:0000256|SAM:MobiDB-lite Q02078 UniProtKB Region 243 270 . . . Note=Disordered;Ontology_term=ECO:0000256;evidence=ECO:0000256|SAM:MobiDB-lite Q02078 UniProtKB Region 266 283 . . . Note=Required for interaction with MAPKs Q02078 UniProtKB Region 289 296 . . . Note=Beta domain Q02078 UniProtKB Region 397 507 . . . Note=Disordered;Ontology_term=ECO:0000256;evidence=ECO:0000256|SAM:MobiDB-lite Q02078 UniProtKB Compositional bias 428 448 . . . Note=Pro residues;Ontology_term=ECO:0000256;evidence=ECO:0000256|SAM:MobiDB-lite Q02078 UniProtKB Compositional bias 450 466 . . . Note=Polar residues;Ontology_term=ECO:0000256;evidence=ECO:0000256|SAM:MobiDB-lite Q02078 UniProtKB Site 176 177 . . . Note=Cleavage;Ontology_term=ECO:0000305;evidence=ECO:0000305 Q02078 UniProtKB Site 213 214 . . . Note=Cleavage;Ontology_term=ECO:0000305;evidence=ECO:0000305 Q02078 UniProtKB Site 466 467 . . . Note=Cleavage;Ontology_term=ECO:0000305;evidence=ECO:0000305 Q02078 UniProtKB Modified residue 59 59 . . . Note=Phosphoserine%3B by CK2;Ontology_term=ECO:0000250;evidence=ECO:0000250 Q02078 UniProtKB Modified residue 98 98 . . . Note=Phosphoserine;Ontology_term=ECO:0007744,ECO:0007744;evidence=ECO:0007744|PubMed:18669648,ECO:0007744|PubMed:23186163;Dbxref=PMID:18669648,PMID:23186163 Q02078 UniProtKB Modified residue 235 235 . . . Note=Phosphoserine;Ontology_term=ECO:0007744;evidence=ECO:0007744|PubMed:18669648;Dbxref=PMID:18669648 Q02078 UniProtKB Modified residue 249 249 . . . Note=N6-acetyllysine;Ontology_term=ECO:0007744;evidence=ECO:0007744|PubMed:19608861;Dbxref=PMID:19608861 Q02078 UniProtKB Modified residue 255 255 . . . Note=Phosphoserine%3B by MAPK14;Ontology_term=ECO:0000269,ECO:0007744,ECO:0007744;evidence=ECO:0000269|PubMed:12586839,ECO:0007744|PubMed:18669648,ECO:0007744|PubMed:23186163;Dbxref=PMID:12586839,PMID:18669648,PMID:23186163 Q02078 UniProtKB Modified residue 312 312 . . . Note=Phosphothreonine%3B by MAPK7 and MAPK14;Ontology_term=ECO:0000269,ECO:0000269,ECO:0000269,ECO:0000269,ECO:0000269;evidence=ECO:0000269|PubMed:10330143,ECO:0000269|PubMed:10849446,ECO:0000269|PubMed:12586839,ECO:0000269|PubMed:17785444,ECO:0000269|PubMed:9858528;Dbxref=PMID:10330143,PMID:10849446,PMID:12586839,PMID:17785444,PMID:9858528 Q02078 UniProtKB Modified residue 312 312 . . . Note=Phosphothreonine%3B by NLK;Ontology_term=ECO:0000269,ECO:0000269,ECO:0000269,ECO:0000269,ECO:0000269;evidence=ECO:0000269|PubMed:10330143,ECO:0000269|PubMed:10849446,ECO:0000269|PubMed:12586839,ECO:0000269|PubMed:17785444,ECO:0000269|PubMed:9858528;Dbxref=PMID:10330143,PMID:10849446,PMID:12586839,PMID:17785444,PMID:9858528 Q02078 UniProtKB Modified residue 319 319 . . . Note=Phosphothreonine%3B by MAPK7 and MAPK14;Ontology_term=ECO:0000269,ECO:0000269,ECO:0000269,ECO:0000269;evidence=ECO:0000269|PubMed:10330143,ECO:0000269|PubMed:10849446,ECO:0000269|PubMed:12586839,ECO:0000269|PubMed:9858528;Dbxref=PMID:10330143,PMID:10849446,PMID:12586839,PMID:9858528 Q02078 UniProtKB Modified residue 355 355 . . . Note=Phosphoserine%3B by MAPK7;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:10849446;Dbxref=PMID:10849446 Q02078 UniProtKB Modified residue 403 403 . . . Note=N6-acetyllysine%3B alternate;Ontology_term=ECO:0000250;evidence=ECO:0000250|UniProtKB:Q2MJT0 Q02078 UniProtKB Modified residue 408 408 . . . Note=Phosphoserine%3B by CDK5;Ontology_term=ECO:0000269,ECO:0000269,ECO:0000269,ECO:0000269;evidence=ECO:0000269|PubMed:12586839,ECO:0000269|PubMed:12691662,ECO:0000269|PubMed:16371476,ECO:0000269|PubMed:16484498;Dbxref=PMID:12586839,PMID:12691662,PMID:16371476,PMID:16484498 Q02078 UniProtKB Modified residue 415 415 . . . Note=Phosphothreonine;Ontology_term=ECO:0000250;evidence=ECO:0000250|UniProtKB:Q60929 Q02078 UniProtKB Modified residue 453 453 . . . Note=Phosphoserine%3B by MAPK;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:9858528;Dbxref=PMID:9858528 Q02078 UniProtKB Cross-link 403 403 . . . Note=Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO)%3B alternate Q02078 UniProtKB Alternative sequence 19 86 . . . ID=VSP_043338;Note=In isoform 7. Missing;Ontology_term=ECO:0000303;evidence=ECO:0000303|PubMed:14702039;Dbxref=PMID:14702039 Q02078 UniProtKB Alternative sequence 19 62 . . . ID=VSP_046018;Note=In isoform 8. VTFTKRKFGLMKKAYELSVLCDCEIALIIFNSSNKLFQYASTDM->TLRKKGLNGCESPDADDYFEHSPLSEDRFSKLNEDSDFIFKRGP;Ontology_term=ECO:0000303;evidence=ECO:0000303|PubMed:15489334;Dbxref=PMID:15489334 Q02078 UniProtKB Alternative sequence 63 132 . . . ID=VSP_046019;Note=In isoform 8. Missing;Ontology_term=ECO:0000303;evidence=ECO:0000303|PubMed:15489334;Dbxref=PMID:15489334 Q02078 UniProtKB Alternative sequence 87 132 . . . ID=VSP_006240;Note=In isoform MEFA%2C isoform RSRFC9%2C isoform 6 and isoform 7. ALNKKEHRGCDSPDPDTSYVLTPHTEEKYKKINEEFDNMMRNHKIA->TLRKKGLNGCESPDADDYFEHSPLSEDRFSKLNEDSDFIFKRGP;Ontology_term=ECO:0000303,ECO:0000303,ECO:0000303,ECO:0000303,ECO:0000303;evidence=ECO:0000303|PubMed:14702039,ECO:0000303|PubMed:1516833,ECO:0000303|PubMed:1748287,ECO:0000303|Ref.2,ECO:0000303|Ref.6;Dbxref=PMID:14702039,PMID:1516833,PMID:1748287 Q02078 UniProtKB Alternative sequence 289 296 . . . ID=VSP_006241;Note=In isoform RSRFC4%2C isoform RSRFC9%2C isoform 5%2C isoform 6 and isoform 8. Missing;Ontology_term=ECO:0000303,ECO:0000303,ECO:0000303,ECO:0000303,ECO:0000303;evidence=ECO:0000303|PubMed:1516833,ECO:0000303|PubMed:15489334,ECO:0000303|PubMed:1748287,ECO:0000303|Ref.2,ECO:0000303|Ref.6;Dbxref=PMID:1516833,PMID:15489334,PMID:1748287 Q02078 UniProtKB Alternative sequence 420 421 . . . ID=VSP_006242;Note=In isoform RSRFC4 and isoform RSRFC9. Missing;Ontology_term=ECO:0000303,ECO:0000303,ECO:0000303;evidence=ECO:0000303|PubMed:1516833,ECO:0000303|PubMed:1748287,ECO:0000303|Ref.2;Dbxref=PMID:1516833,PMID:1748287 Q02078 UniProtKB Natural variant 263 263 . . . ID=VAR_038407;Note=N->S;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:15496429;Dbxref=dbSNP:rs121918530,PMID:15496429 Q02078 UniProtKB Natural variant 279 279 . . . ID=VAR_038408;Note=P->L;Ontology_term=ECO:0000269,ECO:0000269,ECO:0000269;evidence=ECO:0000269|PubMed:15496429,ECO:0000269|PubMed:15958500,ECO:0000269|PubMed:18086930;Dbxref=dbSNP:rs121918529,PMID:15496429,PMID:15958500,PMID:18086930 Q02078 UniProtKB Natural variant 283 283 . . . ID=VAR_038409;Note=G->D;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:15496429;Dbxref=dbSNP:rs121918531,PMID:15496429 Q02078 UniProtKB Natural variant 440 446 . . . ID=VAR_017743;Note=Loss of nuclear localization%3B 66%25 decrease in transcription activation%3B loss of synergistic activation by MEF2A and GATA1 through a dominant-negative mechanism. Missing Q02078 UniProtKB Mutagenesis 176 176 . . . Note=Abolishes cleavage at sites 1 and 2 by caspase 3. Increased cleavage at site 3 by caspase 3. D->A;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:11904443;Dbxref=PMID:11904443 Q02078 UniProtKB Mutagenesis 213 213 . . . Note=Abolishes cleavage at sites 2 and 3 by caspase 7. D->A;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:11904443;Dbxref=PMID:11904443 Q02078 UniProtKB Mutagenesis 255 255 . . . Note=Slightly increased MEF2A protein level. S->A;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:12586839;Dbxref=PMID:12586839 Q02078 UniProtKB Mutagenesis 255 255 . . . Note=Decreased MEF2A protein level. S->D;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:12586839;Dbxref=PMID:12586839 Q02078 UniProtKB Mutagenesis 269 269 . . . Note=Reduced p38 alpha- and beta2-mediated transcriptional activity%3B when associated with A-270. R->A;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:10330143;Dbxref=PMID:10330143 Q02078 UniProtKB Mutagenesis 270 270 . . . Note=Reduced p38 alpha- and beta2-mediated transcriptional activity%3B when associated with A-269. K->A;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:10330143;Dbxref=PMID:10330143 Q02078 UniProtKB Mutagenesis 273 273 . . . Note=Reduced p38 alpha- and beta2-mediated transcriptional activity%3B when associated with A-275. L->A;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:10330143;Dbxref=PMID:10330143 Q02078 UniProtKB Mutagenesis 275 275 . . . Note=Reduced p38 alpha- and beta2-mediated transcriptional activity%3B when associated with A-273. V->A;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:10330143;Dbxref=PMID:10330143 Q02078 UniProtKB Mutagenesis 277 277 . . . Note=Reduced p38 alpha- and beta2-mediated transcriptional activity%3B when associated with A-278. I->A;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:10330143;Dbxref=PMID:10330143 Q02078 UniProtKB Mutagenesis 278 278 . . . Note=Reduced p38 alpha- and beta2-mediated transcriptional activity%3B when associated with A-277. P->A;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:10330143;Dbxref=PMID:10330143 Q02078 UniProtKB Mutagenesis 312 312 . . . Note=Greatly reduced p38-mediated phosphorylation. Abolishes p38-mediated transcriptional activation%3B when associated with A-319. T->A;Ontology_term=ECO:0000269,ECO:0000269;evidence=ECO:0000269|PubMed:10849446,ECO:0000269|PubMed:9858528;Dbxref=PMID:10849446,PMID:9858528 Q02078 UniProtKB Mutagenesis 319 319 . . . Note=Greatly reduced p38-mediated phosphorylation. Abolishes P38-mediated transcriptional activation%3B when associated with A-312. T->A;Ontology_term=ECO:0000269,ECO:0000269;evidence=ECO:0000269|PubMed:10849446,ECO:0000269|PubMed:9858528;Dbxref=PMID:10849446,PMID:9858528 Q02078 UniProtKB Mutagenesis 355 355 . . . Note=No effect on p38-mediated transcriptional activity. S->A;Ontology_term=ECO:0000269,ECO:0000269;evidence=ECO:0000269|PubMed:10849446,ECO:0000269|PubMed:9858528;Dbxref=PMID:10849446,PMID:9858528 Q02078 UniProtKB Mutagenesis 387 387 . . . Note=No effect on p38-mediated phosphorylation. S->A Q02078 UniProtKB Mutagenesis 403 403 . . . Note=Abolishes sumoylation. No change in subcellular location nor in DNA binding. Loss of transcriptional repression. K->R;Ontology_term=ECO:0000269,ECO:0000269;evidence=ECO:0000269|PubMed:16371476,ECO:0000269|PubMed:16563226;Dbxref=PMID:16371476,PMID:16563226 Q02078 UniProtKB Mutagenesis 408 408 . . . Note=Loss of sumoylation. S->A;Ontology_term=ECO:0000269,ECO:0000269;evidence=ECO:0000269|PubMed:12691662,ECO:0000269|PubMed:16371476;Dbxref=PMID:12691662,PMID:16371476 Q02078 UniProtKB Mutagenesis 408 408 . . . Note=Rescues sumoylation. S->D;Ontology_term=ECO:0000269,ECO:0000269;evidence=ECO:0000269|PubMed:12691662,ECO:0000269|PubMed:16371476;Dbxref=PMID:12691662,PMID:16371476 Q02078 UniProtKB Mutagenesis 453 453 . . . Note=No effect on p38-mediated phosphorylation. S->A;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:9858528;Dbxref=PMID:9858528 Q02078 UniProtKB Mutagenesis 479 479 . . . Note=No effect on p38-mediated phosphorylation. S->A;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:9858528;Dbxref=PMID:9858528 Q02078 UniProtKB Sequence conflict 430 430 . . . Note=Missing;Ontology_term=ECO:0000305;evidence=ECO:0000305 Q02078 UniProtKB Helix 14 38 . . . Ontology_term=ECO:0007829;evidence=ECO:0007829|PDB:1EGW Q02078 UniProtKB Beta strand 42 48 . . . Ontology_term=ECO:0007829;evidence=ECO:0007829|PDB:1EGW Q02078 UniProtKB Turn 50 52 . . . Ontology_term=ECO:0007829;evidence=ECO:0007829|PDB:1C7U Q02078 UniProtKB Beta strand 54 60 . . . Ontology_term=ECO:0007829;evidence=ECO:0007829|PDB:1EGW Q02078 UniProtKB Helix 62 71 . . . Ontology_term=ECO:0007829;evidence=ECO:0007829|PDB:1EGW Q02078 UniProtKB Beta strand 77 80 . . . Ontology_term=ECO:0007829;evidence=ECO:0007829|PDB:3KOV Q02078 UniProtKB Helix 81 90 . . . Ontology_term=ECO:0007829;evidence=ECO:0007829|PDB:3P57 Q02078 UniProtKB Modified residue 98 98 . . . Note=Phosphoserine;Ontology_term=ECO:0007744;evidence=ECO:0007744|PubMed:18669648;Dbxref=PMID:18669648 Q02078 UniProtKB Modified residue 98 98 . . . Note=Phosphoserine;Ontology_term=ECO:0007744;evidence=ECO:0007744|PubMed:18669648;Dbxref=PMID:18669648 Q02078 UniProtKB Modified residue 98 98 . . . Note=Phosphoserine;Ontology_term=ECO:0007744;evidence=ECO:0007744|PubMed:18669648;Dbxref=PMID:18669648 Q02078 UniProtKB Modified residue 30 30 . . . Note=Phosphoserine;Ontology_term=ECO:0007744;evidence=ECO:0007744|PubMed:18669648;Dbxref=PMID:18669648 Q02078 UniProtKB Modified residue 30 30 . . . Note=Phosphoserine;Ontology_term=ECO:0007744;evidence=ECO:0007744|PubMed:18669648;Dbxref=PMID:18669648