##gff-version 3
Q8CFN5	UniProtKB	Chain	1	474	.	.	.	ID=PRO_0000199434;Note=Myocyte-specific enhancer factor 2C	
Q8CFN5	UniProtKB	Domain	3	57	.	.	.	Note=MADS-box;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00251	
Q8CFN5	UniProtKB	DNA binding	58	86	.	.	.	Note=Mef2-type;Ontology_term=ECO:0000255;evidence=ECO:0000255	
Q8CFN5	UniProtKB	Region	91	118	.	.	.	Note=Disordered;Ontology_term=ECO:0000256;evidence=ECO:0000256|SAM:MobiDB-lite	
Q8CFN5	UniProtKB	Region	271	278	.	.	.	Note=Beta domain;Ontology_term=ECO:0000250;evidence=ECO:0000250	
Q8CFN5	UniProtKB	Region	368	399	.	.	.	Note=Transcription repressor;Ontology_term=ECO:0000250;evidence=ECO:0000250	
Q8CFN5	UniProtKB	Region	375	474	.	.	.	Note=Disordered;Ontology_term=ECO:0000256;evidence=ECO:0000256|SAM:MobiDB-lite	
Q8CFN5	UniProtKB	Compositional bias	93	118	.	.	.	Note=Basic and acidic residues;Ontology_term=ECO:0000256;evidence=ECO:0000256|SAM:MobiDB-lite	
Q8CFN5	UniProtKB	Compositional bias	375	411	.	.	.	Note=Polar residues;Ontology_term=ECO:0000256;evidence=ECO:0000256|SAM:MobiDB-lite	
Q8CFN5	UniProtKB	Site	433	434	.	.	.	Note=Cleavage;Ontology_term=ECO:0000305;evidence=ECO:0000305	
Q8CFN5	UniProtKB	Modified residue	4	4	.	.	.	Note=N6-acetyllysine;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:18086704;Dbxref=PMID:18086704	
Q8CFN5	UniProtKB	Modified residue	59	59	.	.	.	Note=Phosphoserine%3B by CK2;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:8663403;Dbxref=PMID:8663403	
Q8CFN5	UniProtKB	Modified residue	98	98	.	.	.	Note=Phosphoserine;Ontology_term=ECO:0007744;evidence=ECO:0007744|PubMed:21183079;Dbxref=PMID:21183079	
Q8CFN5	UniProtKB	Modified residue	106	106	.	.	.	Note=Phosphoserine;Ontology_term=ECO:0007744;evidence=ECO:0007744|PubMed:21183079;Dbxref=PMID:21183079	
Q8CFN5	UniProtKB	Modified residue	110	110	.	.	.	Note=Phosphoserine;Ontology_term=ECO:0007744;evidence=ECO:0007744|PubMed:21183079;Dbxref=PMID:21183079	
Q8CFN5	UniProtKB	Modified residue	116	116	.	.	.	Note=N6-acetyllysine;Ontology_term=ECO:0000250;evidence=ECO:0000250|UniProtKB:Q06413	
Q8CFN5	UniProtKB	Modified residue	119	119	.	.	.	Note=N6-acetyllysine;Ontology_term=ECO:0000250;evidence=ECO:0000250|UniProtKB:Q06413	
Q8CFN5	UniProtKB	Modified residue	222	222	.	.	.	Note=Phosphoserine;Ontology_term=ECO:0007744;evidence=ECO:0007744|PubMed:21183079;Dbxref=PMID:21183079	
Q8CFN5	UniProtKB	Modified residue	228	228	.	.	.	Note=Phosphoserine;Ontology_term=ECO:0000250;evidence=ECO:0000250|UniProtKB:Q06413	
Q8CFN5	UniProtKB	Modified residue	234	234	.	.	.	Note=N6-acetyllysine;Ontology_term=ECO:0000250;evidence=ECO:0000250|UniProtKB:Q06413	
Q8CFN5	UniProtKB	Modified residue	239	239	.	.	.	Note=N6-acetyllysine;Ontology_term=ECO:0000250;evidence=ECO:0000250|UniProtKB:Q06413	
Q8CFN5	UniProtKB	Modified residue	240	240	.	.	.	Note=Phosphoserine;Ontology_term=ECO:0007744;evidence=ECO:0007744|PubMed:21183079;Dbxref=PMID:21183079	
Q8CFN5	UniProtKB	Modified residue	252	252	.	.	.	Note=N6-acetyllysine;Ontology_term=ECO:0000250;evidence=ECO:0000250|UniProtKB:Q06413	
Q8CFN5	UniProtKB	Modified residue	264	264	.	.	.	Note=N6-acetyllysine;Ontology_term=ECO:0000250;evidence=ECO:0000250|UniProtKB:Q06413	
Q8CFN5	UniProtKB	Modified residue	293	293	.	.	.	Note=Phosphothreonine%3B by MAPK14;Ontology_term=ECO:0000250;evidence=ECO:0000250|UniProtKB:Q06413	
Q8CFN5	UniProtKB	Modified residue	300	300	.	.	.	Note=Phosphothreonine%3B by MAPK14;Ontology_term=ECO:0000250;evidence=ECO:0000250|UniProtKB:Q06413	
Q8CFN5	UniProtKB	Modified residue	396	396	.	.	.	Note=Phosphoserine%3B by CDK5;Ontology_term=ECO:0000250;evidence=ECO:0000250|UniProtKB:Q06413	
Q8CFN5	UniProtKB	Modified residue	420	420	.	.	.	Note=Phosphoserine%3B by MAPK7;Ontology_term=ECO:0000250;evidence=ECO:0000250|UniProtKB:Q06413	
Q8CFN5	UniProtKB	Modified residue	446	446	.	.	.	Note=Phosphoserine;Ontology_term=ECO:0000250;evidence=ECO:0000250|UniProtKB:Q06413	
Q8CFN5	UniProtKB	Cross-link	391	391	.	.	.	Note=Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO);Ontology_term=ECO:0000250;evidence=ECO:0000250	
Q8CFN5	UniProtKB	Alternative sequence	87	97	.	.	.	ID=VSP_012501;Note=In isoform 4 and isoform 5. TLRKKGLNGCD->ALNKKENKGSE;Ontology_term=ECO:0000303,ECO:0000303;evidence=ECO:0000303|PubMed:15489334,ECO:0000303|PubMed:16141072;Dbxref=PMID:15489334,PMID:16141072	
Q8CFN5	UniProtKB	Alternative sequence	103	118	.	.	.	ID=VSP_012502;Note=In isoform 4 and isoform 5. ADDSVGHSPESEDKYR->SSYALTPRTEEKYK;Ontology_term=ECO:0000303,ECO:0000303;evidence=ECO:0000303|PubMed:15489334,ECO:0000303|PubMed:16141072;Dbxref=PMID:15489334,PMID:16141072	
Q8CFN5	UniProtKB	Alternative sequence	123	134	.	.	.	ID=VSP_012503;Note=In isoform 4 and isoform 5. DIDLMISRQRLC->EFDNMIKSHKIP;Ontology_term=ECO:0000303,ECO:0000303;evidence=ECO:0000303|PubMed:15489334,ECO:0000303|PubMed:16141072;Dbxref=PMID:15489334,PMID:16141072	
Q8CFN5	UniProtKB	Alternative sequence	271	278	.	.	.	ID=VSP_012504;Note=In isoform 2 and isoform 4. Missing;Ontology_term=ECO:0000303,ECO:0000303;evidence=ECO:0000303|PubMed:16141072,ECO:0000303|PubMed:8506376;Dbxref=PMID:16141072,PMID:8506376	
Q8CFN5	UniProtKB	Alternative sequence	368	399	.	.	.	ID=VSP_012505;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	
Q8CFN5	UniProtKB	Mutagenesis	3	3	.	.	.	Note=Increased mobility in differentiating cells. Greatly reduced DNA binding. R->T;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:18086704;Dbxref=PMID:18086704	
Q8CFN5	UniProtKB	Mutagenesis	4	4	.	.	.	Note=7-fold increase in DNA binding. K->Q;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:18086704;Dbxref=PMID:18086704	
Q8CFN5	UniProtKB	Mutagenesis	4	4	.	.	.	Note=Reduced acetylation by 30%25. Some loss of DNA binding and transactivation activity. K->R;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:18086704;Dbxref=PMID:18086704	
Q8CFN5	UniProtKB	Mutagenesis	59	60	.	.	.	Note=Reduced DNA binding activity. ST->CR	
Q8CFN5	UniProtKB	Mutagenesis	59	60	.	.	.	Note=Enhanced DNA binding activity. ST->DD	
Q8CFN5	UniProtKB	Mutagenesis	59	59	.	.	.	Note=Reduced DNA binding activity. S->A;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:8663403;Dbxref=PMID:8663403	
Q8CFN5	UniProtKB	Mutagenesis	59	59	.	.	.	Note=Enhanced DNA binding activity. S->D;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:8663403;Dbxref=PMID:8663403	
Q8CFN5	UniProtKB	Sequence conflict	141	141	.	.	.	Note=F->L;Ontology_term=ECO:0000305;evidence=ECO:0000305	
Q8CFN5	UniProtKB	Sequence conflict	211	211	.	.	.	Note=S->P;Ontology_term=ECO:0000305;evidence=ECO:0000305	
Q8CFN5	UniProtKB	Sequence conflict	428	428	.	.	.	Note=C->S;Ontology_term=ECO:0000305;evidence=ECO:0000305	
Q8CFN5	UniProtKB	Helix	22	38	.	.	.	Ontology_term=ECO:0007829;evidence=ECO:0007829|PDB:5F28	
Q8CFN5	UniProtKB	Beta strand	42	48	.	.	.	Ontology_term=ECO:0007829;evidence=ECO:0007829|PDB:5F28	
Q8CFN5	UniProtKB	Beta strand	54	60	.	.	.	Ontology_term=ECO:0007829;evidence=ECO:0007829|PDB:5F28	
Q8CFN5	UniProtKB	Helix	62	70	.	.	.	Ontology_term=ECO:0007829;evidence=ECO:0007829|PDB:5F28	
Q8CFN5	UniProtKB	Beta strand	77	79	.	.	.	Ontology_term=ECO:0007829;evidence=ECO:0007829|PDB:5F28	
Q8CFN5	UniProtKB	Helix	81	88	.	.	.	Ontology_term=ECO:0007829;evidence=ECO:0007829|PDB:5F28	
Q8CFN5	UniProtKB	Modified residue	108	108	.	.	.	Note=Phosphothreonine;Ontology_term=ECO:0007744;evidence=ECO:0007744|PubMed:21183079;Dbxref=PMID:21183079	
Q8CFN5	UniProtKB	Modified residue	108	108	.	.	.	Note=Phosphothreonine;Ontology_term=ECO:0007744;evidence=ECO:0007744|PubMed:21183079;Dbxref=PMID:21183079